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X-ray Structure of Bacteriorhodopsin at 2.5 Angstroms from Microcrystals Grown in Lipidic Cubic Phases

Pebay-Peyroula, Eva, Rummel, Gabriele, Rosenbusch, Jurg P., Landau, Ehud M.·1997·Science

Abstract

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.

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Metadata

Authors
Pebay-Peyroula, E., Rummel, G., Rosenbusch, J. P., & Landau, E. M.
Venue
Science
Published
1997-09-12
Volume
277
Issue
5332
Pages
1676-1681
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2064497637
Cited by
860
References
0
FWCI
35.58
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: X-ray Structure of Bacteriorhodopsin at 2.5 Angstroms from Microcrystals Grown in Lipidic Cubic Phases. https://app.cochat.ai/papers/10.1126/science.277.5332.1676
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Pebay-Peyroula, E., Rummel, G., Rosenbusch, J. P., & Landau, E. M. (1997). X-ray Structure of Bacteriorhodopsin at 2.5 Angstroms from Microcrystals Grown in Lipidic Cubic Phases. Science. https://doi.org/10.1126/science.277.5332.1676

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