title: Crystallization and preliminary X-ray diffraction analysis of the secreted protein Athe_0614 from Caldicellulosiruptor bescii.
abstract: The Athe_0614 protein is a component of the extracellular proteins secreted by the anaerobic, extremely thermophilic and cellulolytic bacterium Caldicellulosiruptor bescii. The recombinant protein was expressed in Escherichia coli, purified to near-homogeneity and crystallized using polyethylene glycol 2000 monomethyl ether as a precipitant. The crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a = 48.4, b = 42.2, c = 97.8 Å, β = 96.1°, and diffracted to 2.7 Å resolution using synchrotron radiation.
authors.affiliation: Animal Waste Management and Environment Division, National Institute of Livestock and Grassland Science, 2 Ikenodai, Tsukuba, Ibaraki 305-0901, Japan. hiroshiy@affrc.go.jp
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Yokoyama
authors.forename: Takahiro
authors.initials: T
authors.lastname: Yamashita
authors.forename: Naoki
authors.initials: N
authors.lastname: Horikoshi
authors.forename: Hitoshi
authors.initials: H
authors.lastname: Kurumizaka
authors.forename: Wataru
authors.initials: W
authors.lastname: Kagawa
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D016988:Gram-Positive Asporogenous Rods, Irregular / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins
keywords: Caldicellulosiruptor bescii; cellulose; secreted proteins
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