The structure of bacteriorhodopsin at 3.0 A resolution based on electron crystallography: implication of the charge distribution.
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Summary
To evaluate the effect of charges on the density map, a difference (|Fo|-|Fc|) map is calculated including data of a resolution lower than 8.0 A resolution, where the charge effect is significant and strong peaks found in the difference map mainly in the backbone region of the transmembrane helices are interpreted.
- Type
- article
- Published
- 1999-02-26
- Cited by
- 261
- References
- 43
- OpenAlex
- https://openalex.org/W2010622172
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:12142435
Keywords
Bacteriorhodopsin, Chemistry, Resolution (logic), Crystallography, Protonation
References
- Bacteriorhodopsin, a membrane protein that uses light to translocate protons.
- The secondary structure of bacteriorhodopsin determined by Raman and circular dichroism spectroscopy.
- Model building and refinement practice.
- Three-dimensional structure of orthorhombic purple membrane at 6.5 A resolution.
- Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin (*)
- Crystallographic R Factor Refinement by Molecular Dynamics
- Phi/psi-chology: Ramachandran revisited.
- Modification of two peptides of bacteriorhodopsin with a pentaamminecobalt (III) complex.
- Electron-crystallographic refinement of the structure of bacteriorhodopsin.
- PROCHECK: a program to check the stereochemical quality of protein structures
- The CCP4 suite: programs for protein crystallography.
- Examination of the LeafScan 45, a line-illuminating micro-densitometer, for its use in electron crystallography
- On the revised structure of the major phospholipid of Halobacterium salinarium.
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features
- Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212.
- Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin.
- Intramembrane signaling mediated by hydrogen-bonding of water and carboxyl groups in bacteriorhodopsin and rhodopsin.
- A program to produce both detailed and schematic plots of protein structures
- An Apparent Paradox in Crystal Structure Analysis
- Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface.
Cited by
- The structure of aquaporin-1 at 4.5-A resolution reveals short alpha-helices in the center of the monomer.
- Sampling effects influence heights measured with atomic force microscopy
- Structural insights into the mechanism of proton pumping by bacteriorhodopsin
- Lipid–protein interactions in double-layered two-dimensional AQP0 crystals
- Bacteriorhodopsin: Would the real structural intermediates please stand up?
- Prolines in the α-helix confer the structural flexibility and functional integrity of importin-β
- Automation of image processing in electron crystallography.
- X-Ray Crystallography of Bacteriorhodopsin and Its Photointermediates: Insights into the Mechanism of Proton Transport
- Electron crystallography and aquaporins.
- The structure of bacterial S-layer proteins.
- Merging of image data in electron crystallography.
- 3D reconstruction of two-dimensional crystals.
- Electron Microscopy
- 3D reconstruction from 2D crystal image and diffraction data.
- Conformations, flexibility, and interactions observed on individual membrane proteins by atomic force microscopy.
- 4.6 Å Cryo-EM reconstruction of tobacco mosaic virus from images recorded at 300 keV on a 4k × 4k CCD camera
- Design of ordered two-dimensional arrays mediated by noncovalent protein-protein interfaces
- Pattern Recognition of Single-Molecule Force Spectroscopy Data
- Cytoplasmic surface structure of bacteriorhodopsin consisting of interhelical loops and C-terminal alpha helix, modified by a variety of environmental factors as studied by (13)C-NMR.
- 2D Visualisation of SMFS Data on Membrane Proteins
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