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pubmed-article:1404370pubmed:abstractTextX-ray quality single crystals of an extracellular esterase from pathogenic Streptomyces scabies were obtained by the hanging drop method. The crystals are monoclinic (space group C2, a = 161.1 A, b = 51.2 A, c = 124.2 A, beta = 100.6 degrees) with two molecules related by a noncrystallographic dyad in the asymmetric unit, with a solvent content of approximately 64%. The diffraction pattern from fresh crystals extends beyond 2 A resolution using sealed tube CuK alpha radiation. The study has been initiated in order to elucidate the mechanism of this unusual non-serine-dependent esterase, and to gain better understanding of the molecular basis of the pathogenesis of the scab disease.lld:pubmed
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pubmed-article:1404370pubmed:pagination569-71lld:pubmed
pubmed-article:1404370pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1404370pubmed:year1992lld:pubmed
pubmed-article:1404370pubmed:articleTitleCrystallization and preliminary crystallographic data of a Streptomyces scabies extracellular esterase.lld:pubmed
pubmed-article:1404370pubmed:affiliationDepartment of Biochemistry, University of Alberta, Edmonton, Canada.lld:pubmed
pubmed-article:1404370pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1404370pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:1404370pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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