Victor S. Lamzin
European Bioinformatics Institute
149 Papers
1.1K Citations
Victor S. Lamzin is an academic researcher from European Bioinformatics Institute. The author has contributed to research in topics: Chemistry & Active site. The author has an hindex of 46, co-authored 144 publications. Previous affiliations of Victor S. Lamzin include Russian Academy of Sciences.
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Papers
Automated protein model building combined with iterative structure refinement.
TL;DR: Automatic pattern recognition (model building) combined with refinement, allows a structural model to be obtained reliably within a few CPU hours and is demonstrated with examples of a few recently solved structures.
Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7.
TL;DR: ARP/wARP 7.0 tackles several tasks: iterative protein model building including a high-level decision-making control module; fast construction of the secondary structure of a protein; building flexible loops in alternate conformations; fully automated placement of ligands; and finding ordered water molecules.
ARP/wARP and automatic interpretation of protein electron density maps.
TL;DR: This chapter presents phase improvement, coupled with automated map interpretation and model building, as one unified process within the framework of the automated refinement procedure (ARP/wARP) software suite.
554
Crystal Structure of Manganese Catalase from Lactobacillus plantarum
V.V. Barynin,V.V. Barynin,Mei M. Whittaker,Svetlana V. Antonyuk,Victor S. Lamzin,Pauline M. Harrison,Peter J. Artymiuk,James W. Whittaker +7 more
TL;DR: The structure of the mesophilic manganese catalase from Lactobacillus plantarum and its azide-inhibited complex is solved, revealing the existence of two distinct structural classes, differing in monomer design and the organization of their active sites, within theManganeseCatalase family.
332
NAD+-dependent formate dehydrogenase
Vladimir Popov,Victor S. Lamzin +1 more
TL;DR: FDH is perhaps the most suitable model for investigating the general mechanism of catalysis involving hydride ion transfer, and is one of the most promising candidates for the development of so-called coenzyme regeneration systems.