Crystallization and preliminary diffraction analysis of the catalytic domain of xylanase Z from Clostridium thermocellum.
The catalytic domain of a thermostable xylanase from Clostridium thermocellum has been expressed in Escherichia coli and crystallized from a polyethylene glycol 2000 solution by the hanging drop method. Crystals belong to the triclinic space group P1 with cell dimensions a = 46.8 A, b = 50.8 A, c = 70.3 A, alpha = 100.7 degrees, beta = 83.8 degrees, gamma = 101.6 degrees, and two molecules in the unit cell. These crystals diffract X-rays to at least 1.8 A resolution and are suitable for high-resolution X-ray analysis.
Souchon
H
H
Unité d'Immunologie Structurale, URA 359 CNRS, Institut Pasteur, Paris, France.
Spinelli
S
S
Béguin
P
P
Alzari
P M
PM
D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D003013:Clostridium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D043364:Endo-1,4-beta Xylanases; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data
D006026:Glycoside Hydrolases; D043364:Endo-1,4-beta Xylanases