1ap9
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Lipidic cubic phases provide a continuous three-dimensional bilayer matrix | + | Lipidic cubic phases provide a continuous three-dimensional bilayer matrix that facilitates nucleation and growth of bacteriorhodopsin microcrystals. The crystals diffract x-rays isotropically to 2.0 angstroms. The structure of this light-driven proton pump was solved at a resolution of 2.5 angstroms by molecular replacement, using previous results from electron crystallographic studies as a model. The earlier structure was generally confirmed, but several differences were found, including loop conformations and side chain residues. Eight water molecules are now identified experimentally in the proton pathway. These findings reveal the constituents of the proton translocation pathway in the ground state. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Landau, E | + | [[Category: Landau, E M.]] |
[[Category: Pebay-Peyroula, E.]] | [[Category: Pebay-Peyroula, E.]] | ||
| - | [[Category: Rosenbusch, J | + | [[Category: Rosenbusch, J P.]] |
[[Category: Rummel, G.]] | [[Category: Rummel, G.]] | ||
[[Category: RET]] | [[Category: RET]] | ||
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[[Category: retinal protein]] | [[Category: retinal protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:54 2008'' |
Revision as of 09:46, 21 February 2008
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X-RAY STRUCTURE OF BACTERIORHODOPSIN FROM MICROCRYSTALS GROWN IN LIPIDIC CUBIC PHASES
Overview
Lipidic cubic phases provide a continuous three-dimensional bilayer matrix that facilitates nucleation and growth of bacteriorhodopsin microcrystals. The crystals diffract x-rays isotropically to 2.0 angstroms. The structure of this light-driven proton pump was solved at a resolution of 2.5 angstroms by molecular replacement, using previous results from electron crystallographic studies as a model. The earlier structure was generally confirmed, but several differences were found, including loop conformations and side chain residues. Eight water molecules are now identified experimentally in the proton pathway. These findings reveal the constituents of the proton translocation pathway in the ground state.
About this Structure
1AP9 is a Single protein structure of sequence from Halobacterium salinarum with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases., Pebay-Peyroula E, Rummel G, Rosenbusch JP, Landau EM, Science. 1997 Sep 12;277(5332):1676-81. PMID:9287223
Page seeded by OCA on Thu Feb 21 11:46:54 2008
