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Reiner Kiefersauer
Researcher at Max Planck Society
Publications - 29
Citations - 1681
Reiner Kiefersauer is an academic researcher from Max Planck Society. The author has contributed to research in topics: Protein crystallization & Crystal. The author has an hindex of 11, co-authored 28 publications receiving 1530 citations.
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The crystal structure of the proprotein processing proteinase furin explains its stringent specificity.
Stefan Henrich,A. Cameron,A. Cameron,Gleb Bourenkov,Reiner Kiefersauer,Robert Huber,Iris Lindberg,Wolfram Bode,Manuel E. Than +8 more
TL;DR: The 2.6 Å crystal structure of the decanoyl-Arg-Val-Lys- Arg-chloromethylketone (dec-RVKR-cmk)–inhibited mouse furin ectodomain, the first PC structure, reveals an eight-stranded jelly-roll P domain associated with the catalytic domain, which will aid in the rational design of antiviral and antibacterial drugs.
Journal ArticleDOI
Catalysis at a dinuclear [CuSMo(=O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution
TL;DR: The dinuclear [CuSMo(O)OH] cluster of CO dehydrogenase establishes a previously uncharacterized class of dinuclear molybdoenzymes containing the pterin cofactor.
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The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism
Michael Engel,Torsten Hoffmann,Leona Wagner,Michael Wermann,Ulrich Heiser,Reiner Kiefersauer,Robert Huber,Wolfram Bode,Hans-Ulrich Demuth,Hans Brandstetter +9 more
TL;DR: The crystal structure reveals a 2-2-2 symmetric tetrameric assembly which depends on the natively glycosylated β-propeller blade IV and indicates that tetramerization of DP IV is a key mechanism to regulate its interaction with other components.
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Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis
Michael Koch,Constanze Breithaupt,Reiner Kiefersauer,Jörg Freigang,Robert Huber,Albrecht Messerschmidt +5 more
TL;DR: This modelled transmembrane complex provides a structural explanation for the uncoupling of haem biosynthesis observed in variegate porphyria patients and in plants after inhibiting PPO.
Journal ArticleDOI
A novel free-mounting system for protein crystals: transformation and improvement of diffraction power by accurately controlled humidity changes
Reiner Kiefersauer,Manuel E. Than,Holger Dobbek,Lothar Gremer,Marcos Melero,Stefan Strobl,João M. Dias,João M. Dias,Tewfik Soulimane,Robert Huber +9 more
TL;DR: In this paper, a micropipette-based mounting of protein crystals with a controlled stream of air allows an accurate adjustment of the humidity at the crystal, and demonstrates the use of this method in combination with shock-freezing to improve crystal order.