title: Crystallization and preliminary X-ray analysis of a thermophillic Bacillus xylanase.
abstract: A xylanase of M(r) 20,700 from the hyperproductive mutant D3 of the thermophillic Bacillus, strain XE has been purified and crystallized from 2-methyl-2,4-pentanediol. The unit cell is triclinic with a = 48.5 A, b = 51.5 A, c = 72.6 A, alpha = 90.4 degrees, beta = 95.4 degrees, gamma = 92.3 degrees (all +/- 0.2). There are four molecules in the asymmetric unit related by 222 symmetry. These crystals diffract to at least 2.5 A using X-rays from a rotating anode generator.
authors: Protein Engineering Department, AFRC Institute of Food Research, Reading Laboratory, U.K.
authors: R W
authors: RW
authors: Pickersgill
authors: P
authors: P
authors: Debeire
authors: M
authors: M
authors: Debeire-Gosselin
authors: J A
authors: JA
authors: Jenkins
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D003460:Crystallization; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000302:isolation & purification; D006358:Hot Temperature; D014961:X-Ray Diffraction / Q000379:methods; D043325:Xylan Endo-1,3-beta-Xylosidase
chemical_list: D006026:Glycoside Hydrolases; D043325:Xylan Endo-1,3-beta-Xylosidase