Crystallization and preliminary X-ray analysis of the catalytic domain of xylanase a from Pseudomonas fluorescens subspecies cellulosa.
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.
Pickersgill
R W
RW
Protein Engineering Department, AFRC Institute of Food Research Reading Laboratory, Earley Gate, U.K.
Jenkins
J A
JA
Scott
M
M
Connerton
I
I
Hazlewood
G P
GP
Gilbert
H J
HJ
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
D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; D043364:Endo-1,4-beta Xylanases