J
James C. Sacchettini
Researcher at Texas A&M University
Publications - 404
Citations - 35350
James C. Sacchettini is an academic researcher from Texas A&M University. The author has contributed to research in topics: Mycobacterium tuberculosis & Protein structure. The author has an hindex of 77, co-authored 390 publications receiving 32514 citations. Previous affiliations of James C. Sacchettini include Los Alamos National Laboratory & Boston University.
Papers
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Journal ArticleDOI
PHENIX: building new software for automated crystallographic structure determination
Paul D. Adams,Ralf W. Grosse-Kunstleve,Li-Wei Hung,Thomas R. Ioerger,Airlie J. McCoy,Nigel W. Moriarty,Randy J. Read,James C. Sacchettini,Nicholas K. Sauter,Thomas C. Terwilliger +9 more
TL;DR: A novel software package called PHENIX (Python-based Hierarchical ENvironment for Integrated Xtallography) is developed, which will provide the necessary algorithms to proceed from reduced intensity data to a refined molecular model and to facilitate structure solution for both the novice and expert crystallographer.
Journal ArticleDOI
Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase
John D. McKinney,John D. McKinney,John D. McKinney,Kerstin Höner zu Bentrup,Kerstin Höner zu Bentrup,Kerstin Höner zu Bentrup,Ernesto J. Muñoz-Elías,Andras Miczak,Andras Miczak,Bing Chen,Wal Tsing Chan,Dana L. Swenson,Dana L. Swenson,Dana L. Swenson,James C. Sacchettini,William R. Jacobs,David G. Russell,David G. Russell +17 more
TL;DR: It is reported that persistence of M. tuberculosis in mice is facilitated by isocitrate lyase (ICL), an enzyme essential for the metabolism of fatty acids, an observation with important implications for the treatment of chronic tuberculosis.
Journal ArticleDOI
Crystal structure of a plant catechol oxidase containing a dicopper center.
TL;DR: Based on biochemical, spectroscopic and the presented structural data, a catalytical mechanism is proposed in which one of the oxygen atoms of the diphenolic substrate binds to CuB ofThe oxygenated enzyme.
Journal ArticleDOI
Modification of the NADH of the Isoniazid Target (InhA) from Mycobacterium tuberculosis
TL;DR: Data from x-ray crystallography and mass spectrometry reveal that the mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the Nicotinamide ring of nicotinamide adenine dinucleotide bound within the active site of Inh A.
Book ChapterDOI
Automated Structure Solution with the PHENIX Suite
Peter H. Zwart,Pavel V. Afonine,Ralf W. Grosse-Kunstleve,Li-Wei Hung,Thomas R. Ioerger,Airlie J. McCoy,Erik McKee,Nigel W. Moriarty,Randy J. Read,James C. Sacchettini,Nicholas K. Sauter,Laurent C. Storoni,Thomas C. Terwilliger,Paul D. Adams +13 more
TL;DR: The PHENIX software suite as mentioned in this paper is a highly automated system for macromolecular structure determination that can rapidly arrive at an initial partial model of a structure without significant human intervention, given moderate resolution, and good quality data.