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Roberto A. Steiner
Researcher at King's College London
Publications - 50
Citations - 10208
Roberto A. Steiner is an academic researcher from King's College London. The author has contributed to research in topics: Kinesin & Dioxygenase. The author has an hindex of 23, co-authored 50 publications receiving 8763 citations. Previous affiliations of Roberto A. Steiner include University of Padua & University of Groningen.
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Journal ArticleDOI
REFMAC5 for the refinement of macromolecular crystal structures
Garib N. Murshudov,Pavol Skubák,Andrey Lebedev,Navraj S. Pannu,Roberto A. Steiner,Robert A. Nicholls,Winn,Fei Long,Alexei A. Vagin +8 more
TL;DR: The general principles behind the macromolecular crystal structure refinement program REFMAC5 are described.
Journal ArticleDOI
REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use.
Alexei A. Vagin,Roberto A. Steiner,Andrey Lebedev,Liz Potterton,Stuart McNicholas,Fei Long,Garib N. Murshudov +6 more
TL;DR: The organization and some aspects of the use of the using of the flexible and human/machine-readable dictionary of prior chemical knowledge used by the maximum-likelihood macromolecular-refinement program REFMAC5 are described.
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Crystal Structure of the Copper-Containing Quercetin 2,3-Dioxygenase from Aspergillus japonicus
Fabrizia Fusetti,Klaus H Schröter,Roberto A. Steiner,Paula I. van Noort,Tjaard Pijning,Henriëtte J. Rozeboom,Kor H. Kalk,Maarten R. Egmond,Bauke W Dijkstra +8 more
TL;DR: Manual docking of the substrate quercetin into the active site showed that the different geometries of the copper site might be of catalytic importance.
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Anaerobic Enzyme.Substrate Structures Provide Insight Into the Reaction Mechanism of the Copper- Dependent Quercetin 2,3-Dioxygenase.
TL;DR: Structural-based geometric considerations indicate O2 binding to the flavonol C2 atom as the preferred route for flav onol dioxygenation and Glu73 can act as a base in flavonl deprotonation and that it retains the proton.
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Cofactor-independent oxidases and oxygenases.
TL;DR: Cofactor-independent oxygenases and oxidases catalyze very different reactions and belong to several different protein families, reflecting their diverse origin, but all may share the common mechanistic concept of initial base-catalyzed activation of their organic substrate and “substrate-assisted catalysis.”