title: Crystallization and preliminary X-ray analysis of the catalytic domain of xylanase a from Pseudomonas fluorescens subspecies cellulosa.
abstract: The catalytic domain of the xylan-degrading enzyme xylanase A, from Pseudomonas fluorescens subspecies cellulosa, has been expressed in Escherichia coli and crystallized. The crystals are well ordered and diffract to 1.8 A using X-rays generated at the Photon Factory in Japan. The crystals are orthorhombic, space group P2(1)2(1)2(1) with a = 95.7 A, b = 97.1 A and c = 149.8 A (all +/- 0.2 A). The similarity of the a and b cell edges, the intensity of the reflections along c* and the self rotation function results suggest a pseudo-tetragonal arrangement of molecules in the unit cell. There are probably four molecules in the asymmetric unit.
authors.affiliation: Protein Engineering Department, AFRC Institute of Food Research Reading Laboratory, Earley Gate, U.K.
authors.forename: R W
authors.initials: RW
authors.lastname: Pickersgill
authors.forename: J A
authors.initials: JA
authors.lastname: Jenkins
authors.forename: M
authors.initials: M
authors.lastname: Scott
authors.forename: I
authors.initials: I
authors.lastname: Connerton
authors.forename: G P
authors.initials: GP
authors.lastname: Hazlewood
authors.forename: H J
authors.initials: HJ
authors.lastname: Gilbert
mesh_terms: D001665:Binding Sites; D003460:Crystallization; D043364:Endo-1,4-beta Xylanases; D006026:Glycoside Hydrolases / Q000737:chemistry*; D011551:Pseudomonas fluorescens / Q000201:enzymology*; D011994:Recombinant Proteins; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; D043364:Endo-1,4-beta Xylanases