J
Johann Deisenhofer
Researcher at University of Texas Southwestern Medical Center
Publications - 153
Citations - 33597
Johann Deisenhofer is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Photosynthetic reaction centre & Protein structure. The author has an hindex of 80, co-authored 153 publications receiving 32666 citations. Previous affiliations of Johann Deisenhofer include Max Planck Society & University of Texas at Dallas.
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Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution
TL;DR: The molecular structure of the photosynthetic reaction centre from Rhodopseudomonas viridis has been elucidated using X-ray crystallographic analysis and the first description of the high-resolution structure of an integral membrane protein is presented.
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X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
TL;DR: In this paper, an atomic model of the prosthetic groups of the reaction center complex (4 bacteriochlorophyll b, 2 bacteriopheophytin b, 1 non-heme iron, 1 menaquinone, 4 heme groups) was built.
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Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution.
TL;DR: The model of human Fc fragment was refined at 2.9-A resolution and the R value of the model is 0.24, with strong arguments that contact 1 is the fragment B-Fc contact formed in solution under physiological conditions, while contact 2 is a crystal contact.
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Structural mechanism for statin inhibition of HMG-CoA reductase.
Eva S. Istvan,Johann Deisenhofer +1 more
TL;DR: The structures of the catalytic portion of human HMGR complexed with six different statins are determined, which show several catalytically relevant residues are disordered in the enzyme-statin complexes.
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The leucine-rich repeat: a versatile binding motif.
Bostjan Kobe,Johann Deisenhofer +1 more
TL;DR: The crystal structure of ribonuclease inhibitor protein has revealed that leucine-rich repeats correspond to beta-alpha structural units, which are arranged so that they form a parallel beta-sheet with one surface exposed to solvent, so that the protein acquires an unusual, nonglobular shape.