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Crystallization and preliminary diffraction analysis of the catalytic domain of xylanase Z from Clostridium
H Souchon1, S Spinelli, P Béguin
1Unité d'Immunologie Structurale, URA 359 CNRS, Institut Pasteur, Paris, France.
Abstract:
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.
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