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Richard Henderson

Researcher at Laboratory of Molecular Biology

Publications -  190
Citations -  27543

Richard Henderson is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Bacteriorhodopsin & Cryo-electron microscopy. The author has an hindex of 67, co-authored 185 publications receiving 26018 citations. Previous affiliations of Richard Henderson include University of Hertfordshire & Medical Research Council.

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Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy.

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.
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Three-dimensional model of purple membrane obtained by electron microscopy

TL;DR: A 7-Å resolution map of the purple membrane has been obtained by electron microscopy of tilted, unstained specimens and shows that Lipid bilayer regions fill the spaces between the protein molecules.
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Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy.

TL;DR: The hand determination and refinement optimization procedure is applied to image pairs of the dihydrolipoyl acetyltransferase (E2) catalytic core of the pyruvate dehydrogenase complex from Bacillus stearothermophilus taken by low-dose electron cryomicroscopy.
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Structure of a beta1-adrenergic G-protein-coupled receptor.

TL;DR: G-protein-coupled receptors have a major role in transmembrane signalling in most eukaryotes and many are important drug targets and here the 2.7 Å resolution crystal structure of a β1-adrenergic receptor in complex with the high-affinity antagonist cyanopindolol is reported.
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Molecular structure determination by electron microscopy of unstained crystalline specimens.

TL;DR: The projected structures of two unstained periodic biological specimens, the purple membrane and catalase, have been determined by electron microscopy to resolutions of 7 A and 9 A, respectively.