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dc.contributor.authorZhao, Haiyan
dc.contributor.authorTang, Liang
dc.date.accessioned2015-05-05T20:33:43Z
dc.date.available2015-05-05T20:33:43Z
dc.date.issued2009-04-01
dc.identifier.citationZhao, H., & Tang, L. (2009). Crystallographic characterization of the histidine protein kinase from an essential two-component regulatory system YycFG. Acta Crystallografica F Struct Biol Cryst Commun., 64(4), 346-349. http://www.dx.doi.org/10.1107/S174430910900668Xen_US
dc.identifier.urihttp://hdl.handle.net/1808/17600
dc.descriptionThis is the publisher's version, also available electronically from "http://scripts.iucr.org".en_US
dc.description.abstractYycGF is a highly conserved two-component signal transduction system that is specific to low-G+C Gram-positive bacteria, including many important human pathogens. It has been recognized as a crucial regulatory system for cell-wall metabolism. YycG, the histidine protein kinase of this system, is a multidomain transmembrane protein. The truncated cytoplasmic portion of YycG from Bacillus subtilis encompassing the PAS domain, the dimerization domain and the catalytic domain was expressed, purified and crystallized. X-ray data were collected to 2.8 Å resolution with a completeness of 98.2% and an overall Rmerge of 5.6%. The crystals belonged to space group P61 or P65, with unit-cell parameters a = 135.0, c = 133.0 Å. The selenomethionine-substituted version of the protein was crystallized and X-ray data were collected to 3.6 Å resolution for subsequent MAD phasing.en_US
dc.publisherInternational Union of Crystallographyen_US
dc.subjecthistidine protein kinasesen_US
dc.subjectTwo-component systemsen_US
dc.subjectSignal transductionen_US
dc.subjectGram-positive bacteriaen_US
dc.subjectcell wallen_US
dc.subjectPAS domainsen_US
dc.subjectYycGen_US
dc.subjectYycFen_US
dc.subjectAutophosphorylationen_US
dc.titleCrystallographic characterization of the histidine protein kinase from an essential two-component regulatory system YycFGen_US
dc.typeArticle
kusw.kuauthorTang, Liang
kusw.kudepartmentMolecular Biosciencesen_US
dc.identifier.doi10.1107/S174430910900668X
kusw.oaversionScholarly/refereed, publisher version
kusw.oapolicyThis item meets KU Open Access policy criteria.
dc.rights.accessrightsopenAccess


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