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pubmed-article:18540059pubmed:dateCreated2008-6-9lld:pubmed
pubmed-article:18540059pubmed:abstractTextAdenosine triphosphate (ATP) binding cassette transporters (ABC transporters) are ATP hydrolysis-dependent transmembrane transporters. Here, the overproduction, purification and crystallization of the putative ABC transporter ATP-binding protein TM0222 from Thermotoga maritima are reported. The protein was crystallized in the hexagonal space group P6(4)22, with unit-cell parameters a = b = 148.49, c = 106.96 A, gamma = 120.0 degrees . Assuming the presence of two molecules in the asymmetric unit, the calculated V(M) is 2.84 A(3) Da(-1), which corresponds to a solvent content of 56.6%. A three-wavelength MAD data set was collected to 2.3 A resolution from SeMet-substituted TM0222 crystals. Data sets were collected on the BL38B1 beamline at SPring-8, Japan.lld:pubmed
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pubmed-article:18540059pubmed:authorpubmed-author:SinghTej PTPlld:pubmed
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pubmed-article:18540059pubmed:pagination498-500lld:pubmed
pubmed-article:18540059pubmed:dateRevised2010-11-18lld:pubmed
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pubmed-article:18540059pubmed:articleTitlePurification, crystallization and preliminary X-ray diffraction analysis of the putative ABC transporter ATP-binding protein from Thermotoga maritima.lld:pubmed
pubmed-article:18540059pubmed:affiliationDepartment of Biophysics, All India Institute of Medical Sciences, Ansari Nagar, New Delhi 110 029, India.lld:pubmed
pubmed-article:18540059pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18540059pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed