Crystallization and preliminary X-ray diffraction analysis of crystals of Thermoascus aurantiacus xylanase.
Crystals suitable for high resolution X-ray diffraction analysis have been grown of the 29,774-Da protein, xylanase (1,-4-beta-xylan xylanohydrolase EC 3.2.1.8) from the thermophilic fungus Thermoascus aurantiacus. This protein, an endoxylanase demonstrates the hydrolysis of beta-(1-4)-D-xylose linkage in xylans and crystallizes as monoclinic pinacoids in the presence of ammonium sulphate buffered at pH 6.5, and also with neutral polyethylene glycol 6000. The crystals belong to space group P2(1) and have cell dimensions, a = 41.2 A, b = 67.76 A, c = 51.8 A; beta = 113.2 degrees.
Viswamitra
M A
MA
Department of Physics, Indian Institute of Science, Bangalore.
Bhanumoorthy
P
P
Ramakumar
S
S
Manjula
M V
MV
Vithayathil
P J
PJ
Murthy
S K
SK
Naren
A P
AP
D001203:Ascomycota / Q000201:enzymology*; D003460:Crystallization; D006026:Glycoside Hydrolases / Q000737:chemistry*; D014961:X-Ray Diffraction; D043325:Xylan Endo-1,3-beta-Xylosidase
D006026:Glycoside Hydrolases; D043325:Xylan Endo-1,3-beta-Xylosidase