Author
J. Lepault
Bio: J. Lepault is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Contrast transfer function & Tilt (optics). The author has an hindex of 1, co-authored 1 publications receiving 687 citations.
Papers
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TL;DR: In this article, the strength of the very weak high-resolution Fourier components of the image of a two-dimensional crystal was determined using real space correlation analysis, and the amplitude and phase information was extracted from the distortion-corrected image of the crystal.
694 citations
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TL;DR: A complete atomic model for bacteriorhodopsin between amino acid residues 8 and 225 has been built and suggests that pK changes in the Schiff base must act as the means by which light energy is converted into proton pumping pressure in the channel.
2,772 citations
TL;DR: EMAN (Electron Micrograph ANalysis), a software package for performing semiautomated single-particle reconstructions from transmission electron micrographs, was written from scratch in C++ and is provided free of charge on the Web site.
2,551 citations
TL;DR: The structure of the light-harvesting chlorophyll a/b–protein complex, an integral membrane protein, has been determined at 3.4 Å resolution by electron crystallography of two-dimensional crystals.
Abstract: The structure of the light-harvesting chlorophyll a/b-protein complex, an integral membrane protein, has been determined at 3.4 A resolution by electron crystallography of two-dimensional crystals. Two of the three membrane-spanning alpha-helices are held together by ion pairs formed by charged residues that also serve as chlorophyll ligands. In the centre of the complex, chlorophyll a is in close contact with chlorophyll b for rapid energy transfer, and with two carotenoids that prevent the formation of toxic singlet oxygen.
1,801 citations
TL;DR: An atomic model of human red cell AQP1 is described, providing a possible molecular explanation to a longstanding puzzle in physiology—how membranes can be freely permeable to water but impermeable to protons.
Abstract: Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues that permit rapid water transport, whereas the water selectivity is due to a constriction of the pore diameter to about 3 A over a span of one residue. The atomic model provides a possible molecular explanation to a longstanding puzzle in physiology-how membranes can be freely permeable to water but impermeable to protons.
1,662 citations
TL;DR: Two computer programs are presented, CTFFIND3 and CTFTILT, which determine defocus parameters from images of untilted specimens, as well as defocus and tilt parameters from image of tilted specimens, respectively, using a simple algorithm.
1,480 citations