R
Robert Huber
Researcher at Agricultural & Applied Economics Association
Publications - 329
Citations - 26772
Robert Huber is an academic researcher from Agricultural & Applied Economics Association. The author has contributed to research in topics: Protein structure & Multiple isomorphous replacement. The author has an hindex of 78, co-authored 311 publications receiving 25131 citations. Previous affiliations of Robert Huber include Swiss Federal Institute for Forest, Snow and Landscape Research & Munich University of Applied Sciences.
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Journal ArticleDOI
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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Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins.
Robert Huber,Carrell Rw +1 more
TL;DR: Article synthese sur l'α1-antitrypsine: caracteristiques structurales and fonctionnelles (capacite de liaison a des modulateurs) andrology en tant que modele pour toutes les serpines.
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The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.
TL;DR: A stoichiometric complex formed between human alpha‐thrombin and D‐Phe‐Pro‐Arg chloromethylketone was crystallized in an orthorhombic crystal form in full agreement with published cDNA sequence data.
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The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex.
TL;DR: The described structure of a soluble Fcγ receptor (sFcγRIII, CD16), an Fc fragment from human IgG1 (hFc1) and their complex is a model for immune complex recognition and helps to explain the vastly differing affinities of other F cγR–IgG complexes and the FcεRIα-IgE complex.
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Human α1-proteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
TL;DR: Two closely related crystal structures of alpha 1-proteinase inhibitor modified at the reactive site peptide bond Met358--Ser359 have been analysed, indicating a major structural rearrangement upon modification of the intact inhibitor.