Membrane Proteins of Known Structure

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Last database update: 3 July 2009

New Structures:
AdiC Amino acid antiporter
yeast Aqy1 aquaporin at 1.15 Å resolution
Sulfide:quinone oxidoreductase
Photosystem II. Br-substitution shows location of chlorides

Unique proteins* in database = 196.

Number of coördinate files in database = 480.

*Includes proteins of same type from different species. For example, photosynthetic reaction centers from R. viridis and R. sphaeroides are considered unique. Structures of mutagenized versions of proteins already in the database are excluded as unique. Proteins that differ only by substrate bound or by physiological state are also excluded. Structures 'obsoleted' by the PDB are not included. The figure to the right shows the progress of membrane protein structure determination. The figure may be used freely in seminar presentations provided that the URL and lab information on the image are not removed. We thank Ahmed Bakan for bringing some counting errors to our attention.

This database emphasizes structures determined by diffraction methods, although some NMR structures are included. A comprehensive list of NMR-determined structures is available from Dror Warschawski.

Membrane Proteins of Known 3D Structure
(Table description)
Protein	PDB Code	Reference (links are to PubMed)
MONOTOPIC MEMBRANE PROTEINS
*Prostaglandin H2 synthase-1: Ram (Ovine) seminal vesicle, 3.5 Å*	1PRH	Picot et al. (1994)
*Cyclooxygenase-2: Mus Musculus, 3.0Å*	1CX2	Kurumbail et al. (1996)
*Squalene-hopene cyclase: Alicyclobacillus acidocaldarius, 2.0 Å* 2SQC is space group P4₃2₁2. 3SQC, 2.8 Å is P3₂21.	2SQC	Wendt et al. (1999)
*Monoamine Oxidase B: Human mitochondrial outer membrane (expressed in Pichia pastoris), 3.0 Å* NOTE: MAOB has a single transmembrane helix that anchors it to the outer membrane (residues 489-515). Nevertheless, we consider it monotopic because the bulk of the 520 residue protein, including the active site, is outside of the membrane.	1GOS	Binda et al. (2002)
*Monoamine Oxidase B with bound Isatin: Human mitochondrial outer membrane (expressed in Pichia pastoris), 1.70 Å* with bound Tranylcypromine, 2.20 Å: 1OJB with bound N-(2-aminoethyl)-p-chlorobenamide, 2.40 Å: 1OJC with bound Lauryldimethyl-amine N-Oxide, 3.10 Å: 1OJD with bound 1.4-Diphenyl-2-butene, 2.30 Å: 1OJ9	1OJA	Binda et al. (2003)
*Monoamine Oxidase A with bound Clorglycine: Human mitochondrial outer membrane (expressed in Pichia pastoris), 3.00 Å* crystal form B, 3.15 Å: 2BXS Monoamine Oxidase B with bound Deprenyl, 2.20 Å: 2BYB	2BXR	De Colibus et al. (2005)
*Monoamine Oxidase A with bound Harmine: Human mitochondrial outer membrane (expressed in S. cerevisiae), 2.20 Å* G110A mutant with bound Harmine, 2.17 Å: 2Z5Y	2Z5X	Son et al. (2008)
*Monoamine Oxidase A: Rat mitochondrial outer membrane (expressed in S. cerevisiae), 3.20 Å*	1O5W	Ma et al. (2004)
*Fatty acid amide hydrolase: Rattus norvegicus, 2.8 Å* NOTE: Like MAO, FAAH has a single TM segment. But the active site is external to the membrane, and many other residues on the protein surface contribute to membrane binding. Absence of the TM segment affects neither membrane association or function.	1MT5	Bracey et al. (2002)
*Flavoprotein-ubiquinone oxidoreductase (ETF-QO) with bound UQ: Sus scrofa, 2.5 Å* UQ-free structure, 2.6 Å: 2GMJ	2GMH	Zhang et al. (2006)
*Sulfide:quinone oxidoreductase in complex with decylubiquinone: Aquifex aeolicus, 2.0 Å* "as-purified" protein, 2.30 Å: 3H27 in complex with aurachin C, 2.9 Å: 3H29 This monotopic membrane protein is thought to be buried about 12 Å in the bilayer interface. Also listed under Respiratory Proteins.	3H28	Marcia et al. (2009)
*Peptidoglycan Glycosyltransferase: Staphylococccus aureus, 2.8 Å* NOTE: The enzyme has a single TM segment, which is absent in the structure. The active site is external to the membrane, but the so-called Jaw Region contributes to membrane binding. 2OLV shows the enzyme complexed with moenomycin. 2OLU is the structure of the apoenzyme.	2OLV	Lovering et al. (2007)
*Peptidoglycan Glycosyltransferase penicillin-binding protein 1a (PBP1a): Aquifex aeolicus* (Expressed in E. coli), 2.1 Å** NOTE: The enzyme has a single TM segment, which is absent in the structure. The active site is external to the membrane.	2OQO	Yuan et al. (2007)
*Peptidoglycan Glycosyltransferase penicillin-binding protein 1b (PBP1b): Escherichia coli, 2.16 Å* NOTE: The single TM segment is present in this structure. The active site is external to the membrane. SeMet Protein, 3.09 Å: 3FWL	3FWM	Sung et al. (2009)
*Signal Peptide Peptidase (SppA), native protein: Eschericia coli, 2.55 Å* SeMet protein, 2.76 Å: 3BEZ. Long thought to be a transmembrane protein, the structure reveals a peripheral homotetramer that likely is buried in the membrane interface. Each monomer has a putative N-terminal transmembrane helix for anchoring to the membrane. This anchor was removed for crystallization. Also listed under Intramembrane Proteases.	3BF0	Kim et al. (2008)
*Glycerol-3-phosphate dehydrogenase (GlpD, native): Escherichia coli, 1.75 Å* SeMet-GlpD, 1.95 Å: 2R4J GlpD-2-PGA, 2.3 Å: 2R45 GlpD-PEP, 2.1 Å: 2R46 GlpD-DHAP, 2.1 Å: 2R4E Also listed under Respiratory Proteins.	2QCU	Yeh et al. (2008)
*ADP-ribosylation factor (ARF1), myristoylated: Saccharomyces cerevisiae* (Expressed in E. coli), NMR Structure**	2K5U	Yeh et al. (2008)
TRANSMEMBRANE PROTEINS: BETA-BARREL
Beta-Barrel Membrane Proteins: Multimeric (Porins and Relatives)
*Porin: Rhodobacter capsulatus, 1.8 Å*	2POR	Weiss & Schulz (1992)
*Porin: Rhodopeudomonas blastica,* 1.96 Å**	1PRN	Kreutsch et al. (1994)
*OmpK36 osmoporin: Klebsiella pneumoniae, 3.2 Å*	1OSM	Dutzler et al. (1999)
*Omp32 anion-selective porin: Comamonas acidovorans, 2.1 Å*	1E54	Zeth et al. (2000)
*Omp32 anion-selective porin: Delftia acidovorans, 1.5 Å* With bound malate, 1.45 Å: 2FGQ	2FGR	Zachariae et al. (2006)
*OmpF Matrix Porin: Escherichia coli, 2.4 Å* Note: Also see BtuB with bound colicin E3 R-domain, below.	2OMF	Cowan et al. (1992)
*OmpF Matrix Porin: Escherichia coli, 1.6 Å* With inserted 83 residue N-terminal peptide of colicin E3, 3.0 Å: 2ZLD	2ZFG	Yamashita et al. (2008)
*OmpC Osmoporin: Escherichia coli, 2.0 Å*	2J1N	Baslé et al. (2006)
*OmpG monomeric* porin: Escherichia coli, 2.3 Å**	2F1C	Subbarao and van den Berg (2006)
*OmpG monomeric* porin in open state: Escherichia coli, 2.3 Å** OmpG in closed state, 2.73 Å: 2IWW	2IWV	Yildiz et al. (2006)
*OmpG monomeric* porin: Escherichia coli, NMR Structure (DPC micelles)**	2JQY	Liang & Tamm (2007)
*PhoE: Escherihia coli, 3.0 Å*	1PHO	Cowan et al. (1992)
*LamB Maltoporin : Salmonella typhimurium, 2.4 Å*	2MPR	Meyer et al. (1997)
*LamB Maltoporin: Escherichia coli,* 3.1 Å**	1MAL	Schirmer et al. (1995)
*ScrY sucrose-specific porin: Salmonella typhimurium, 2.4 Å* Complexed Form, 1AOT. Uncomplexed form, 1A0S.	1A0T	Forst et al. (1998)
*MspA mycobacterial porin: Mycobacterium smegmatis, 2.5 Å* Homooctamer	1UUN	Faller et al. (2004)
*OprP phosphate-specific transporter: Pseudomonas aeruginosa, 1.9 Å* Contains a novel nine-residue arginine ladder	2O4V	Moraes et al. (2007)
*OprD basic amino acid uptake channel: Pseudomonas aeruginosa, 2.9 Å* Like OprP, contains a basic ladder	2ODJ	Biswas et al. (2007)
*OpdK hydrocarbon transporter: Pseudomonas aeruginosa, 2.8 Å* Binds vanillate. Forms labile trimer.	2QTK	Biswas et al. (2008)
Beta-Barrel Membrane Proteins: Monomeric/Dimeric
*TolC outer membrane protein: Escherichia coli,* 2.1 Å** NOTE: Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel.	1EK9	Koronakis et al.(2000)
*VceC outer membrane protein: Vibrio cholerae,* 1.8 Å** NOTE: Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel.	1YC9	Federici et al. (2005)
*OprM drug discharge outer membrane protein: Pseudomonas aeruginosa,* 2.56 Å** NOTE: Functional protein is a homotrimer. Each monomer contributes 4 strands to a single barrel.	1WP1	Akama et al. (2004)
*apo BtuB cobalamin transporter: Escherichia coli, 2.0 Å* Related structures: 1NQF (SeMet-BtuB), 1NQG (Ca²⁺-BtuB), 1NQH (Ca²⁺-B₁₂-BtuB).	1NQE	Chimento et al.(2003)
*apo BtuB by in meso* crystallization: Escherichia coli, 1.95 Å** NOTE: Crystals were prepared from cubic phase lipids. This is the first β-barrel protein prepared by this method.	2GUF	Cherezov et al. (2006)
*BtuB with bound colicin E3 R-domain: Escherichia coli, 2.75 Å* NOTE: The 135-residue coiled-coil R-domain is believed to deliver the colicin to OmpF (above).	1UJW	Kurisu et al. (2003)
*BtuB with bound colicin E2 R-domain: Escherichia coli, 3.50 Å* NOTE: The 135-residue coiled-coil R-domain is believed to deliver the colicin to OmpF or OmpC (above).	2YSU	Sharma et al. (2007)
*BtuB in complex with TonB: Escherichia coli, 2.1 Å*	2GSK	Shultis et al. (2006)
*Colicin I receptor Cir in complex with Colicin Ia binding domain: Escherichia coli, 2.5 Å* Cir Colicin I receptor alone, 2.65 Å: 2HDF	2HDI	Buchanan et al. (2007)
*OmpA: Escherichia coli, x-ray diffraction, 2.5 Å*	1BXW	Pautsch & Schulz (1998)
*OmpA: Escherichia coli, x-ray diffraction, 1.6 Å*	1QJP	Pautsch & Schulz (2000)
*OmpA: Escherichia coli, NMR (in DPC micelles)*	1G90	Arora et al. (2001)
*OmpA with four shortened loops: Escherichia coli, NMR (in DHPC micelles)* Called β-barrel platform (BBP)	2JMM	Johansson et al. (2007)
*OmpT outer membrane protease: Escherichia coli, 2.6 Å*	1I78	Vandeputte-Rutten et al. (2001)
*OmpW outer membrane protein: Escherichia coli, 2.7 Å* 2F1V is orthorhomibic form. Trigonal form, 3.0 Å: 2F1T	2F1V	Hong et al. (2006)
*OmpX: Escherichia coli, 1.9 Å* Structure at 2.1 Å, 1QJ9	1QJ8	Vogt & Schulz (1999)
*OmpX: Escherichia coli, NMR (DHPC micelles)*	1ORM	Fernández et al. (2001)
*OmpX: Escherichia coli, NMR (DPC micelles, with H-bond constraints)* For structure without H-bond constraints, see 1Q9G	1Q9F	Fernández et al. (2004)
*TtoA Outer Membrane Protein (OMP): Thermus thermophilus* HB27, 2.8 Å** First structure of an OMP from a thermophile	3DZM	Brosig et al. (2009)
*OmpLA outer membrane phospholipase A monomer: Escherichia coli,* 2.17 Å** Dimer, 2.10 Å: 1QD6	1QD5	Snijder et al.(1999)
*OpcA adhesin protein: Neisseria meningitidis, 2.0 Å*	1K24	Prince et al. (2002)
NspA surface protein: Neisseria meningitidis, 2.55 Å	1P4T	Vandeputte-Rutten et al. (2003)
*NalP autotransporter translocator domain: Neisseria meningitidis, 2.60 Å* p6₁22 space group. See also 1UYO, C222₁ space group, 3.2 Å resolution.	1UYN	Oomen et al.(2004)
*Hia_1022-1098 trimeric autotransporter: Haemophilus influenzae, 2.0 Å* Hia_992-1098, 2.3 Å: 2GR7	2GR8	Meng et al. (2006)
*EspP autotransporter, postcleavage state: Escherichia coli, 2.7 Å*	2QOM	Barnard et al. (2007)
*PagP outer membrane palimitoyl transferease: Escherichia coli, NMR* 1MM4 is Structure in DPC micelles. Structure in OG micelles: 1MM5	1MM4	Hwang et al. (2002)
*PagP outer membrane palimitoyl transferease: Escherichia coli, x-ray, 1.9 Å*	1THQ	Ahn et al. (2004)
*FadL long-chain fatty acid transporter: Escherichia coli, 2.6 Å* 1T16 is from Monoclinic crystals. From hexagonal crystals, 2.8 Å: 1T1L	1T16	van den Berg et al. (2004)
*FadL long-chain fatty acid transporter A77E/S100R mutant: Escherichia coli, 2.5 Å* Mutants show that channel wall opening for passage of fatty acids into inner layer of outer membrane is likely. P34A mutant, 3.3 Å: 2R4L N33A mutant, 3.2 Å: 2R4N ΔNPA mutant, 3.6 Å: 2R4O G212E mutant, 2.9 Å: 2R4P	3DWN	Hearn et al. (2009)
*FadL homologue long-chain fatty acid transporter: Pseudomonas aeruginosa* (expressed in E. coli), 2.2 Å** Shows break in channel wall for passage of fatty acids into inner layer of outer membrane in a species other than E. coli. Residues 22-463.	3DWO	Hearn et al. (2009)
*FauA alcaligin outer membrane transporter: Bordetella pertusssis* (expressed in E. coli), 2.3 Å**	3EFM	Brillet et al. (2009)
*TodX hydrocarbon transporter: Pseudomonas putida, 2.6 Å* 3BS0 is P1 space group, 2 molecules in asymmetric unit. I222 space group, 3.2 Å: 3BRZ	3BS0	Hearn et al. (2008)
*TbuX hydrocarbon transporter: Ralstonia pickettii, 3.2 Å*	3BRY	Hearn et al. (2008)
*Tsx nucleoside transporter (apoprotein): Eschericia coli, 3.0 Å* Protein + thymidine, 3.10 Å: 1TLW Protein + uridine, 3.10 Å: 1TLZ	1TLY	Ye and van den Berg (2004)
*FhuA, Ferrichrome-iron receptor without ligand: Escherichia coli, 2.7 Å* With ligand: 1BY5	1BY3	Locher et al. (1998)
*FhuA-AW140-LPS: Escherichia coli, 2.5 Å* Detailed examination of the structure of lipopolysaccharide (LPS) in complex with FhuA. FhuA-DL41-LPS-ferricrocin, 2.7 Å: 1QFF	1QFG	Ferguson et al. (2000)
*FhuA in complex with lipopolysaccharide and rifamycin CGP4832 Escherichia coli, 2.90 Å*	1FI1	Ferguson et al. (2001)
*FhuA: Escherichia coli,* 2.5 Å**	2FCP	Ferguson et al. (1998)
*FhuA + ferrichrome-iron: Escherichia coli,* 2.7 Å**	1FCP	Ferguson et al. (1998)
*FhuA in complex withTonB: Escherichia coli, 3.3 Å*	2GRX	Pawelek et al. (2006)
*FepA, Ferric enterobactin receptor: Escherichia coli, 2.4 Å*	1FEP	Buchanan et al. (1999)
*FecA, siderophore transporter: Escherichia coli,* 2.0 Å** Structure at 2.5 Å: 1KMP	1KMO	Ferguson et al. (2002)
*FecA, siderophore transporter periplasmic signalling domain: Escherichia coli,* NMR Structure** Shows the signalling domain not seen x-ray structures	2D1U	Garcia-Herrero & Vogel (2005)
*FecA, siderophore transporter (no ligand): Escherichia coli,* 2.5 Å** FecA with iron-free dicitrate, 2.15 Å: : 1PO0 FecA with diferric dicitrate, 3.4 Å: : 1PO3	1PNZ	Yue et al. (2003)
*HasR heme-uptake receptor in complex with HasA hemophore and heme: Serratia marcescens* (Expressed in E. coli), 2.7 Å** HasA~HasR, 3.0 Å: 3CSN HasA~HasR[I671G]~heme, 2.8 Å: 3DDR	3CSL	Krieg et al. (2009)
*FptA, pyochelin outer membrane receptor: Pseudomonas aeruginosa, 2.0 Å*	1XKW	Cobessi et al. (2005)
*FpvA, Pyoverdine receptor: Pseudomonas aeruginosa, 3.6 Å*	1XKH	Cobessi et al. (2005)
*FpvA, Pyoverdine receptor (apo form): Pseudomonas aeruginosa, 2.77 Å*	2O5P	Brillet et al. (2007)
*P pilus usher translocation domain, PapC_130-640: Escherichia coli, 3.2 Å*	2VQI	Remaut et al. (2008)
Beta-Barrel Membrane Proteins: Mitochondrial Outer Membrane
*VDAC-1 voltage dependent anion channel (Human expressed in E. coli) NMR structure* Structure determined in LDAO micelles.	2K4T	Hiller et al.(2008)
*VDAC-1 voltage dependent anion channel (Human expressed in E. coli): 4 Å* Structure determined by combining x-ray and NMR data.	2JK4	Bayrhuber et al.(2008)
*VDAC-1 voltage dependent anion channel (Murine expressed in E. coli): 2.3 Å* Reveals the voltage-sensing N-terminal α-helix.	3EMN	Ujwal et al.(2008)
Omp85-TpsB Outer Membrane Transporter Superfamily
*FhaC Filamentous Hemagglutinin Transporter: Bordetella pertussis, 3.15 Å* The first outer membrane protein from the Omp85–two-partner secretion B (TpsB) superfamily	2QDZ	Clantin et al. (2007)
*YaeT_21-351 POTRA domains (periplasmic fragment): Escherichia coli, 2.2 Å* The polypeptide transport-associated (POTRA) domains link to a transmembrane β-barrel, which is absent in this structure.	2QCZ	Kim et al. (2007)
*YaeT_21-410 POTRA domains (periplasmic fragment): Escherichia coli, 3.3 Å* The polypeptide transport-associated (POTRA) domains link to a transmembrane β-barrel, which is absent in this structure. Structure shows the first four POTRA domains in an extended conformation.	3EFC	Gatzeva-Topalova et al. (2008)
Non-constitutive. Pore-forming Toxins, etc.
*Alpha-hemolysin: Staphylococcus aureus, 1.9 Å*	7AHL	Song et al. (1996)
*LukF: Staphylococcus aureus, 1.9 Å* NOTE: The structure is of the water soluble form of the protein. It is included here because it is similar to alpha-hemolysin in behavior, and may be taken as representative of the protomeric state of alpha-hemolysin. At 2.5 Å: 2LKF. With bound phosphocholine, 1.9 Å: 3LKF	1LKF	Olson et al. (1999)
TRANSMEMBRANE PROTEINS: ALPHA-HELICAL
Non-constitutive. Alpha-helical Pore-forming Toxins, etc.
*Cytolysin A (ClyA, aka HlyE): Escherichia coli, 3.29 Å*	2WCD	Mueller et al. (2009)
Outer Membrane Proteins
*Wza translocon for capsular polysaccharides: Escherichia coli, 2.25 Å* The first outer membrane protein that penetrates the membrane as an alpha-helix bundle. The intact protein is comprised of eight monomers.	2J58	Dong et al. (2006)
*Porin B monomer: Corynebacterium glutamicum* expressed in Escherichia coli, 1.82 Å** Putative helical porin, probably comprised of five monomers. Crystal form I. Crystal form II, 2.89 Å: 2VQH Crystal form IV, 4.20 Å: 2VQK Crystal form III, 3.16 Å: 2VQL	2VQG	Ziegler et al. (2008)
Bacterial Rhodopsins Halobacterium salinarium if not noted otherwise.
Bacteriorhodopsin (BR)
2D crystals, electron diffraction, 3.5 Å	2BRD	Grigrorieff et al. (1996)
2D crystals, electron diffraction, 3.0 Å	1AT9	Kimura et al. (1997)
3D crystals, X-ray, 2.35 Å	1AP9	Pebay-Peyroula et al. (1997)
3D crystals, X-ray, 1.9 Å	1QHJ	Belrhali et al. (1999)
K intermediate: 3D crystals, X-ray, 2.1 Å R-free = O.255. 1QKO, 2.1 Å has R-free = 0.303	1KQP	Edman et al. (1999)
3D crystals, X-ray, 2.3 Å	1BRX	Luecke et al. (1998)
3D crystals, X-ray, 1.55 Å	1C3W	Luecke et al. (1999)
D96N mutant in bR state: 3D crystals, X-ray, 1.80 Å D96N mutant in M-state, 2.00 Å: 1C8S.	1C8R	Luecke et al. (1999)
3D crystals, X-ray, 2.9 Å	1BRR	Essen et al. (1998)
Halorhodopsin (HR)
3D crystals, X-ray, 1.8 Å	1E12	Kolbe et al. (2000)
Sensory Rhodopsin I (SRI)
*3D crystals, X-ray, 2.0 Å, Anabaena (Nostoc)* sp. PCC7120**	1XIO	Vogeley et al. (2004)
Sensory Rhodopsin II (SRII)
3D crystals, X-ray, 2.4 Å, N. pharaonis	1JGJ	Luecke et al. (2001)
3D crystals, X-ray, 2.1 Å, N. pharaonis	1H68	Royant et al. (2001)
Sensory Rhodopsin II with Transducer
3D crystals, X-ray, 1.93 Å, N. pharaonis	1H2S	Gordeliy et al. (2002)
Archaerhdopsins
Archaerhodopsin-1 (aR-1), x-ray, 3.4 Å, Halorubrum sp. aus -1	1UAZ	Enami et al. (2006)
Archaerhodopsin-2 (aR-2), x-ray, 2.5 Å, Haloroubrum sp. aus -2	1VGO	Enami et al. (2006)
Archaerhodopsin-2 (aR-2), x-ray, 2.10 Å, Haloroubrum sp. aus-2 Crystallized with the carotenoid bacterioruberin. 2EI4 is space group P321. Space group P6₃: 2Z55, 2.50 Å.	2EI4	Yoshimura & Kouyama. (2008)
Xanthorhodopsin
Xanthorhodopsin with bound carotenoid, x-ray, 1.9 Å, Salinibacter ruber	3DDL	Luecke et al. (2008)
G Protein-Coupled Receptors
Rhodopsin: Bovine Rod Outer Segment, 2.8 Å. See also 1HZX	1F88	Palczewski et al. (2000)
Rhodopsin: Bovine Rod Outer Segment, 2.6 Å	1L9H	Okada et al. (2002)
Rhodopsin: Bovine Rod Outer Segment, 2.65 Å	1GZM	Li et al. (2004)
Rhodopsin: Bovine Rod Outer Segment, 2.2 Å	1U19	Okada et al. (2004)
Rhodopsin: Bovine Rod Outer Segment (expressed in COS cells), 3.4 Å Recombinant rhodopsin mutant, N2C/D282C	2J4Y	Standfuss et al. (2007)
Rhodopsin, photoactivated: Bovine Rod Outer Segment, 4.15 Å Ground state, rhombohedral crystals, 3.8 Å 2I35. Ground state, trigonal crystals, 4.1 Å 2I36.	2I37	Salom et al. (2006)
Rhodopsin in ligand-free state (opsin): Bovine Rod Outer Segment, 2.9 Å 2 molecules in asymmetric unit.	3CAP	Park et al. (2008)
*Rhodopsin, Ops-GαCT peptide complex: Bovine Rod Outer Segment, 3.2 Å**	3DQB	Scheerer et al. (2008)
*Rhodopsin: Squid (Todarodes pacificus), 2.5 Å*	2Z73	Murakami & Kouyama (2008)
*Rhodopsin: Squid (Todarodes pacificus), 3.7 Å* Shows intracellularly extended cytoplasmic region.	2ZIY	Shimamura et al. (2008)
Turkey β₁ adrenergic receptor (engineered), 2.7 Å Expressed in baculovirus.	2VT4	Warne et al. (2008)
Human β₂ adrenergic receptor, 3.4/3.7 Å from β₂AR365-Fab5 complex. From β₂AR24/365-Fab5 complex: 2R4S	2R4R	Rasmussen et al. (2007)
Engineered human β₂ adrenergic receptor, 2.4 Å T4 lysozyme replaces third intracellular loop. Reveals close association with cholesterol.	2RH1	Cherezov et al. (2007)
Engineered human β₂ adrenergic receptor, 2.8 Å T4 lysozyme replaces third intracellular loop. Reveals specific cholesterol binding site.	3D4S	Hanson et al. (2008)
Human A_2A adenosine receptor, 2.6 Å In complex with a high-affinity subtype-selective antagonist ZM241385.	3EML	Jaakola et al. (2008)
Autonomously Folding "Membrane Proteins" (Sec-independent)
*Mistic membrane-integrating protein, Bacillus subtilis. NMR structure* Note: This is not a constitutive membrane protein. It is included here because of general interest.	1YGM	Roosild et al. (2005)
Ion Channels (more information)
*KcsA Potassium channel, H⁺ gated: Streptomyces lividans* (Expressed in E. coli), 3.2 Å**	1BL8	Doyle et al. (1998)
*KcsA Potassium channel, H⁺ gated: Streptomyces lividans* (Expressed in E. coli), 2.0 Å** R-free = 0.233. 1K4D, 2.3 Å, R-free = 0.235	1K4C	Zhou et al. (2001)
*Full-length KcsA Potassium channel, H⁺ gated: Streptomyces lividans* (Expressed in E. coli), 3.80 Å** Crystallized with synthetic Fab2 antibodies. C-terminal domain alone (residues 129-158) crystallized with synthetic Fab4 antibodies 3EFD, 2.60 Å	3EFF	Uysal et al. (2009)
*NaK channel (Na⁺complex): Bacillus cereus* (expressed in E. coli), 2.4 Å** K⁺ complex, 2.8 Å: 2AHZ.	2AHY	Shi et al. (2006)
*NaK (NΔ19) channel in the open state: Bacillus cereus* (expressed in E. coli), 1.6 Å**	3E86	Alam & Jiang (2009)
*MthK Potassium channel, Ca⁺⁺ gated: Methanobacterium* thermoautotrophicum, 3.3 Å**	1LNQ	Jiang et al. (2002) Crystal structure and mechanism. Jiang et al. (2002) Open pore conformation.
*KvAP Voltage-gated potassium Channel: Aeropyrum pernix, 3.2 Å* Voltage sensor domain, 1.9 Å: 1ORS	1ORQ	Jiang et al (2003) Crystal structures. Jiang et al (2003) Voltage sensor mechanism.
*KirBac1.1 Inward-Rectifier Potassium channel (closed state): Burkholderia pseudomallei, 3.65 Å*	1P7B	Kuo et al (2003)
*Kir3.1-Prokaryotic Kir Chimera: Mus musculus & Burkholderia xenovornas,* 2.2 Å** Expressed in Escherichia coli.	2QKS	Nishida et al (2007)
*KirBac3.1 Inward-Rectifier Potassium channel (intermediate states): Magnetospirillum magnetotacticum, 2.6 Å* 1XL4 is "intermediate state" 1. "Intermediate state" 2, 2.85 Å: 1XL6	1XL4	Gulbis, J.M., Kuo, A., Smith, B., Doyle, D.A., Edwards, A., Arrowsmith, C., Sundstrom, M., in preparation
*Kv1.2 Voltage-gated potassium Channel: Rattus norvegicus* (expressed in Pichia pastoris) , 2.9 Å**	2A79	Long et al. (2005a) Long et al. (2005b)
*Kv1.2/Kv2.1 Voltage-gated potassium channel chimera: Rattus norvegicus* (expressed in Pichia pastoris) , 2.4 Å** First Kv channel with resolved lipids.	2R9R	Long et al. (2007)
*MlotiK1 cyclic nucleotide-regulated K⁺-channel: Mesorhizobium loti* (expressed in E. coli) , 3.1 Å**	3BEH	Clayton et al. (2008)
Influenza M2 proton channel (synthesized), 2.05 Å with amantadine inhibitor, 3.50 Å: 3C9J	3BKD	Stouffer et al. (2008)
Influenza M2 proton channel (bacterial expression system), NMR structure with rimantadine inhibitor	2RLF	Schnell & Chou. (2008)
*mGIRK1 G-Protein Gated Inward Rectifying Potassium Channel: Mus musculus, 1.8 Å* NOTE: This is not strictly an integral membrane protein, because it is the cytoplasmic channel domain located external to the membrane. It is included here for completeness.	1N9P	Nishida & MacKinnon (2002)
*ASIC1 Acid-Sensing Ion Channel: Gallus gallus, 1.9 Å*	2QTS	Jasti et al. (2007)
*Nicotinic Acetylcholine Receptor Pore (closed state): Torpedo marmorata, electron diffraction, 4.0 Å*	1OED	Miyazawa et al. (2003)
*Nicotinic Acetylcholine Receptor, refined structure: Torpedo marmorata, electron diffraction, 4.0 Å*	2BG9	Unwin (2005)
*Prokaryotic pentameric ligand-gated ion channel (pLGIC): Erwinia chrysanthemi* (expressed in E. coli), 3.3 Å** First high-resolution x-ray structure of an AChR-like channel.	2VL0	Hilf & Dutzler (2008)
*Prokaryotic pentameric ligand-gated ion channel (GLIC): Gloebacter violaceus* (expressed in E. coli), 3.1 Å** Related to pLGIC (above), this pentameric channel is apparently in an open state. E221A mutant, 3.50 Å: 3EI0	3EHZ	Hilf & Dutzler (2009)
*Prokaryotic pentameric ligand-gated ion channel (GLIC): Gloebacter violaceus* (expressed in E. coli), 2.9 Å** Related to pLGIC (above), this pentameric channel is apparently in an open state.	3EAM	Bocquet et al. (2009)
*MscL Mechanosensitive channel: Mycobacterium tuberculosis, 3.5 Å*	2OAR	Chang et al. (1998)
*MscS voltage-modulated mechanosensitive channel: Escherichia coli,* 3.7 Å**	2OAU	Bass et al. (2002)
*MscS mechanosensitive channel in the open form: Escherichia coli,* 3.45 Å**	2VV5	Wang et al. (2008)
*CorA Mg²⁺ Transporter: Thermotoga maritima, 3.9 Å* Soluble domain, 1.85 Å. 2BBH	2BBJ	Lunin et al. (2006)
*CorA Mg²⁺ Transporter: Thermotoga maritima, 2.9 Å*	2IUB	Eshaghi et al. (2006)
*MgtE Mg²⁺ Transporter: Thermus thermophilus, 3.5 Å* Cytoplasmic domains w. bound Mg²⁺, 2.30 Å: 2YVY Cytoplasmic domains without Mg²⁺, 3.90 Å: 2YVZ	2YVX	Hattori et al. (2007)
Other Channels: Protein-Conducting
*SecYEβ protein-conducting channel: Methanococcus jannaschii, 3.5 Å* Coördinates of native complex: 1RHZ. Coördinates of double-mutant complex (K422R,V423T) 1RH5 (3.2 Å resolution).	1RHZ	van den Berg et al. (2004)
*SecYEβ protein-conducting channel with full-plug (TM2a) deletion: Methanococcus jannaschii, 3.6 Å* Coördinates of mutant with half-plug deletion 2YXQ (3.5 Å resolution).	2YXR	Li et al. (2007)
*SecYEG protein-conducting channel in complex with SecA: Thermotoga maritima* (expressed in E. coli), 4.5 Å**	3DIN	Zimmer et al. (2008)
*SecYE protein-conducting channel in complex with a Fab fragment: Thermus thermophilus* (expressed in E. coli), 3.20 Å** SecYE alone 2ZQP (6.0 Å resolution).	2ZJS	Tsukazaki et al. (2008)
Other Channels: Aquaporins and Glyceroporins
AQP0 aquaporin water channel: Bovine lens, 2.24 Å	1YMG	Harries et al. (2004)
AQP0 aquaporin water channel: Ovine lens, electron diffraction, 3.0 Å (plane) by 3.5 Å (normal) AQP0 organized as a membrane junction.	1SOR	Gonen et al. (2004)
AQP0 aquaporin lens junction: Ovine lens, electron diffraction, 1.9 Å Non-junctional form, 2.4 Å: 2B6P	2B6O	Gonen et al. (2005)
AQP1 aquaporin water channel: Human red blood cell, electron diffraction, 3.8 Å (in membrane plane)	1FQY	Murata et al. (2000)
AQP1 aquaporin water channel: Human red blood cell, in vitreous ice by electron diffraction, 3.7 Å	1IH5	Ren et al. (2001)
AQP1 aquaporin water channel: Bovine red blood cell, X-ray diffraction, 2.2 Å	1J4N	Sui et al. (2001)
AQP4 aquaporin water channel: rat glial cells (expressed in insect cells), electron diffraction, 3.2 Å	2D57	Hiroaki et al. (2005)
AQP4 aquaporin water channel: rat glial cells (expressed in insect cells), electron diffraction, 2.8 Å S180D mutant. Structure reveals five lipids associated with AQP4.	2ZZ9	Tani et al. (2009)
*AQP4 aquaporin water channel: Human (expressed in Pichia pastoris), 1.8 Å*	3GD8	Ho et al. (2009)
*AQP5 aquaporin water channel (HsAQP5): human (expressed in Pichia pastoris): 2.0 Å*	3D9S	Horsefield et al. (2008)
*AQPZ aquaporin water channel: Escherichia coli, 2.5 Å*	1RC2	Savage et al. (2003)
*AQPZ aquaporin showing two conformations of Arg-189: Escherichia coli, 3.2 Å*	2ABM	Jiang et al. (2006)
*SoPIP2;1 plant aquaporin: Spinacia oleracea* (expressed in Pichia pastoris) 2.1 Å** 1Z98 is closed conformation. Open conformation, 3.9 Å: 2B5F	1Z98	Törnroth-Horsefield et al. (2006)
*GlpF glycerol facilitator channel: Escherichia coli,* 2.2 Å**	1FX8	Fu et al. (2000)
*GlpF glycerol facilitator channel, W84F/F200T-mutant: Escherichia coli,* 2.1 Å** GlpF with non-transported xylose replacing glycerol: (GlpF - G)_A, 2.7 Å: 1LDI GlpF with non-transported xylose replacing glycerol: (GlpF - G)_B, 2.8 Å: 1LDA	1LDF	Tajkhorshid et al. (2002)
*PfAQP aquaglyceroporin: Plasmodium falciparum,* 2.05 Å** Transports water and glycerol equally well.	3C02	Newby et al. (2008)
*Aqy1 yeast aquaporin (pH 3.5): Pischia pastoris, 1.15 Å* pH 8.0, 1.40 Å: 2W1P	2W2E	Fischer et al. (2009)
Other Channels: Gap Junctions
Connexin 26 (Cx26; GJB2) gap junction: Human (expressed in Sf9 cells), 3.5 Å	2ZW3	Maeda et al. (2009)
Other Channels: Amt/Rh proteins
*AmtB ammonia channel (mutant): Escherichia coli,* 1.40 Å** 1U7G is Protein + ammonia. Apoprotein, 2.0 Å: 1U77 Protein + methylammonia, 1.85 Å: 1U7C	1U7G	Khademi et al. (2004)
*AmtB ammonia channel (wild-type): Escherichia coli,* 1.8 Å (P6₃ crystal form)** R3 crystal form: 1XQE, 2.1 Å resolution	1XQF	Zheng et al. (2004)
*AmtB ammonia channel in complex with GlnK: Escherichia coli,* 2.5 Å**	2NUU	Conroy et al. (2007)
*AmtB ammonia channel in complex with inhibitory GlnK: Escherichia coli,* 1.96 Å**	2NS1	Gruswitz et al. (2007)
*Amt-1 ammonium channel: Archaeoglobus fulgidus,* 1.54 Å** Native protein: 2B2F. Protein + 20 mM Ammonium Sulfate: 2B2H Protein + 80 mM Ammonium Sulfate: 2B2I Protein+xenon: 2B2J	2B2F	Andrade et al. (2005)
*Rh protein, possible ammonia or CO₂ channel: Nitrosomonas europaea,* 1.85 Å** CO₂ pressurized protein, 1.85 Å: 3B9Z	3B9Y	Li et al. (2007)
*Rh protein, possible ammonia or CO₂ channel: Nitrosomonas europaea,* 1.30 Å**	3B9W	Lupo et al. (2007)
Intramembrane Proteases ( NSMB News & Views on three GlpG Structures)
*GlpG rhomboid-family intramembrane protease: Eschericia coli, 2.1 Å* P3₂ space group. One molecule in asymmetric unit.	2IC8	Wang et al. (2006)
*GlpG rhomboid-family intramembrane protease: Eschericia coli, 2.5 Å* Shows GlpG in a more open conformation.	2O7L	Wang & Ha (2007)
*GlpG rhomboid-family intramembrane protease: Eschericia coli, 2.6 Å* P3₁ space group. Two anti-parallel molecules in asymmetric unit.	2NRF	Wu et al. (2006)
*GlpG rhomboid-family intramembrane protease: Eschericia coli, 2.3 Å* P2₁ space group. Two anti-parallel molecules in asymmetric unit.	2IRV	Ben-Shem et al. (2007)
*GlpG rhomboid-family intramembrane peptidase: Haemophilus influenzae, 2.2 Å* Shows three bound lipid molecules. Monoclinic C2 space group.	2NR9	Lemieux et al. (2007)
*Site-2 Protease (S2P). Intramembrane Metalloprotease: Methanocaldococcus jannaschii, 3.3 Å* Structure is of the transmembrane core only.	3B4R	Feng et al. (2007)
*Signal Peptide Peptidase (SppA), native protein: Eschericia coli, 2.55 Å* SeMet protein, 2.76 Å: 3BEZ. Long thought to be a transmembrane protein, the structure reveals a peripheral homotetramer that likely is buried in the membrane interface. Each monomer has a putative N-terminal transmembrane helix for anchoring to the membrane. This anchor was removed for crystallization. Also listed under Monotopic Membrane Proteins.	3BF0	Kim et al. (2008)
H⁺/Cl^- Exchange Transporters
*H⁺/Cl^- Exchange Transporter (formerly ClC Chloride Channel), Salmonella typhimurium,* 3.0 Å** Eschericia coli, 3.5 Å: 1KPK	1KPL	Dutzler et al. (2002)
H⁺/Cl^- Exchange Transporter (formerly ClC Chloride Channel) *Gating by a glutamate residue: Escherichia coli,* 2.51 Å** Glu148Ala mutant, 1OTT. Glu148Gln mutant, 1OTU.	1OTS	Dutzler et al. (2003)
Multi-Drug Efflux Transporters
*AcrB bacterial multi-drug efflux transporter: Escherichia coli, 3.5 Å*	1IWG	Murakami et al. (2002)
*AcrB bacterial multi-drug efflux transporter in complex with bile acid: Escherichia coli, 3.85 Å*	2W1B	Drew et al. (2008)
*AcrB bacterial multi-drug efflux transporter: Escherichia coli, 3.7 Å* With substrates: 1OY8, 1OY9, 1OYD, 1OYE	1OY6	Yu et al. (2003)
*AcrB bacterial multi-drug efflux transporter: Escherichia coli, 2.9 Å* Two crystal forms. C2: 2GIF. P1: 2HRT, 3.0 Å. Together, the two forms suggest a pump mechanism.	2GIF	Seeger et al. (2006)
*AcrB bacterial multi-drug efflux transporter with substrates: Escherichia coli, 2.8 Å* 2DHH is without ligand w. minocycline: 2DRD, 3.1 Å w. doxorubicin: 2DR6, 3.3 Å	2DHH	Murakami et al. (2006)
*AcrB bacterial multi-drug efflux transporter with YajC subunit: Escherichia coli, 3.5 Å*	2RDD	Törnroth-Horsefield et al. (2007)
*MexB bacterial multi-drug efflux transporter: Pseudomonas aeruginosa* (expressed in E. coli), 3.0 Å**	2V50	Sennhauser et al. (2009)
*EmrE bacterial multi-drug efflux transporter with bound TPP substrate: Escherichia coli, 3.8 Å* 3B5D is C2 crystal form. P2₁ form with TPP, 4.5 Å: 3B62 3B5D and 3B62 expressed in cell-free system. Ligand-free structure expressed in vivo, 4.5 Å: 3B61	3B5D	Chen et al. (2007)
Membrane-Associated Proteins in Eicosanoid and Gluththione Metabolism (MAPEG)
*Microsomal Glutathione Transferase 1: Rattus norvegicus, 3.2 Å* (Electron Diffraction)	2H8A	Holm et al. (2006)
*Microsomal Prostaglandin E Synthase 1: Human (Expressed in E. coli), 3.5 Å* (Electron Diffraction) In complex with glutathione.	3DWW	Jegerschöld et al. (2008)
*5-Lipoxygenase-Activating Protein (FLAP) with Bound MK-591 Inhibitor: Human, 4.0 Å* FLAP with iodinated MK-591 analog: 2Q7R. Expressed in E. coli.	2Q7M	Ferguson et al. (2007)
*Leukotriene LTC₄ Synthase in complex with glutathione: Human, 3.3 Å* Expressed in Shizosaccharomyces pombe.	2PNO	Ago et al. (2007)
*Leukotriene LTC₄ Synthase in complex with glutathione: Human, 2.15 Å* apo form: 2UUI, 2.00 Å. Expressed in Pichia pastoris.	2UUH	Molina et al. (2007)
Major Facilitator Superfamily (MSF) Transporters
*LacY Lactose Permease Transporter (C154G mutant): Escherichia coli, 3.6 Å* 1PV7 is with bound high-affinity lactose homolog, TDG. See 1PV6 for structure without TDG (3.5 Å).	1PV7	Abramson et al. (2003)
*LacY Lactose Permease (C154G mutant) without substrate at 2 pH values: Escherichia coli, 2.95 Å* 2CFQ structure determined at pH 6.5. 2CFP structure determined at pH 5.6 (3.30 Å).	2CFQ	Mirza et al. (2006)
*LacY Lactose Permease (wild-type) with TDG: Escherichia coli, 3.6 Å*	2V8N	Guan et al. (2007)
*GlpT Glycerol-3-Phosphate Transporter: Escherichia coli, 3.3 Å*	1PW4	Huang et al. (2003)
*EmrD Multidrug Transporter: Escherichia coli, 3.5 Å*	2GFP	Yin et al. (2006)
Solute Sodium Symporter (SSS) Family
*vSGLT Sodium Galactose Transporter: Vibrio parahaemolyticus, 2.70 Å*	3DH4	Faham et al. (2008)
Nucleobase-Cation-Symport-1 (NCS1) Family
*Mhp1 Benzyl-hydantoin transporter (without substrate): Microbacterium liquefaciens* (Expressed in E. coli), 2.85 Å** With hydantion substrate 2JLO (4.0 Å).	2JLN	Weyand et al. (2008)
Betaine/Choline/Carnitine Transporter (BCCT) Family
*BetP glycine betaine transporter: Corynebacterium glutamicum* (Expressed in E. coli), 3.35 Å** A Na⁺-coupled symporter in an intermediate state.	2W8A	Ressl et al. (2009)
Amino Acid/Polyamine/Organocation (APC) Superfamily
*AdiC Arginine:Agmatine Antiporter (P2₁2₁2₁ space group): Escherichia coli, 3.6 Å* P1 space group: 3H6B, 4.1 Å.	3H5M	Gao et al. (2009)
Amino Acid Secondary Transporters
*LeuT_Aa Leucine transporter: Aquifex aeolicus* (expressed in E. coli), 1.65 Å**	2A65	Yamashita et al. (2005)
LeuT Leucine transporter with bound inhibitors: Aquifex aeolicus (expressed in E. coli), 1.85 Å Alanine-Sodium-Clomipramine Leucine-Sodium-Clomipramine, 2Q6H Leucine-Sodium-Imipramine, 2Q72 Leucine-Sodium-Desipramine, 2QB4	2QEI	Singh et al. (2007)
*LeuT Leucine transporter with bound Na⁺ and tryptophan: Aquifex aeolicus* (expressed in E. coli), 2.00 Å**. Shows the transporter in an open-to-out conformation. w. bound glycine, 2.15 Å: 3F4J w. bound alanine, 1.90 Å: 3F48 w. bound leucine (30mM), 1.80 Å: 3F3E w. bound methionine, 1.90 Å: 3F3D w. bound selenomethionine, 1.95 Å: 3F4I w. bound 4-fluorophenylalanine, 2.10 Å: 3F3C	3F3A	Singh et al. (2009)
*LeuT Leucine Transporter with Bound Desipramine: Aquifex aeolicus* (expressed in E. coli), 2.9 Å**	2QJU	Zhou et al. (2007)
*Wild-type LeuT transporter with bound octylglucopyranoside (OG): Aquifex aeolicus* (expressed in E. coli), 2.0 Å** E290S mutant with bound OG, 2.8 Å: 3JGC	3GJD	Quick et al. (2009)
*Glutamate Transporter Homologue (Glt_Ph): Pyrococcus horikoshii* (expressed in E. coli), 3.5 Å**	1XFH	Yernool et al. (2004)
*Aspartate Transporter Li⁺-Bound State(Glt_Ph): Pyrococcus horikoshii* (expressed in E. coli), 2.96 Å** TBOA-bound, 3.20 Å: 2NWW Sodium-bound, 3.29 Å: 2NWX	2NWL	Boudker et al. (2007)
Cation Diffusion Facilitator (CDF) Family
*YiiP Zinc Transporter: Escherichia coli, 3.8 Å* Renamed FieF iron & zinc transporter (see Grass et al. Arch. Microbiol. 183:9-18, 2005)	2QFI	Lu & Fu (2007)
Antiporters
*NhaA Na⁺/H⁺ antiporter: Escherichia coli, 3.45 Å*	1ZCD	Hunte et al. (2005)
*NhaA Na⁺/H⁺ antiporter: Escherichia coli* by electron crystallography** Difference maps show structural changes with changes in pH.	3FI1	Appel et al. (2009)
Mitochondrial ADP/ATP Carrier: Bovine heart mitochondria, 2.2 Å Monomeric, in complex with carboxyatractyloside inhibitor. Also listed under Respiratory Proteins.	1OKC	Pebay-Peyroula et al. (2003)
Mitochondrial ADP/ATP Carrier: Bovine heart mitochondria, 2.8 Å Biological dimer with endogenous cardiolipins. Also listed under Respiratory Proteins.	2C3E	Nury et al. (2005)
ATP Binding Cassette Transporters
*BtuCD Vitamin B₁₂ Transporter: Escherichia coli, 3.2 Å*	1L7V	Locher et al. (2002)
*Sav1866 Multidrug Transporter: Staphylococcus aureus, 3.0 Å*	2HYD	Dawson and Locher (2006)
*BtuCD-F Complex; BtuCD B₁₂ Transporter + BtuF binding protein: Escherichia coli, 2.6 Å*	2QI9	Hvorup et al. (2007)
*Molybdate Transporter ModB₂C₂ Complexed with ModA: Archaeoglobus fulgidus, 3.1 Å* ModA with bound MoO₄, 1.60 Å 2ONR ModA with bound WO₄, 1.55 Å 2ONS	2ONK	Hollenstein et al. (2007)
*ModBC Molybdate ABC Transporter in a trans-inhibited state: Methanosarcina acetivorans, 3.0 Å*	3D31	Gerber et al. (2008)
*HI1470/1 Putative Metal-Chelate-type ABC Transporter: Haemophilus influenzae, 2.4 Å* First structure showing an inward-facing conformation of an ABC transporter	2NQ2	Pinkett et al. (2007)
*MsbA Lipid "flippase" with bound AMPPNP: Salmonella typhimurium* (expressed on E. coli), 3.7 Å** MsbA with bound AMPPNP used for initial model: 3B5Y, 4.5 Å ADP + Vanadate-bound conformation: 3B5Z, 4.2 Å Open apo-conformation (E. coli): 3B5W, 5.3 Å Closed apo-conformation (Vibrio cholerae expressed in E. coli): 3B5X, 5.5 Å	3B60	Ward et al. (2007)
*P-Glycoprotein: Mus musculus* (mouse, expressed in Pichia pastoris), 3.8 Å** With bound QZ59-RRR: 3G60, 4.40 Å With bound QZ59-SSS: 3G61, 4.35 Å	3G5U	Aller et al. (2009)
*MalFGK₂-MBP Maltose uptake transporter complex: Escherichia coli, 2.8 Å* Complex includes maltose-binding protein (MBP), maltose, and ATP	2R6G	Oldham et al. (2007)
*MalFGK₂ uptake transporter: Escherichia coli, 4.5 Å* Helix TM1 deleted. Shows transporter in the inward conformation in the resting state.	3FH6	Khare et al. (2009)
*MetNI Methionine uptake transporter complex: Escherichia coli, 3.7 Å* MetN-C2 domain 3DHX, 2.1 Å	3DHW	Kadaba et al. (2008)
Hydrolases
Estrone Sulfatase: Human placenta, 2.6 Å	1P49	Hernandez-Guzman et al. (2003)
Oxygenases
*Particulate methane monooxgenase (pMMO): Methylococcus capsulatus, 2.8 Å*	1YEW	Lieberman & Rosenzweig (2005)
Photosynthetic Reaction Centers
Rhodopseudomonas virdis, 2.3 Å The first high-resolution crystallographic structure of a membrane protein	1PRC

from the Stephen White laboratory at UC Irvine

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Useful Membrane Protein Structure Resources

Progress of membrane protein structure determination. See also Carpenter et al. (2008)

Hartmut Michel's Database of Membrane Protein Crystallization

European Membrane Protein Consortium

Martin Caffrey's Membrane Protein Data Bank (University of Limerick)

Bilayer Insertion of Membrane Proteins (Structural Bioinformatics and Computational Biochemistry Unit, Oxford)

Protein Data Bank of Transmembrane Proteins (Institute of Enzymology, Budapest)