Crystallization and Preliminary Diffraction Analysis of the Catalytic Domain of Xylanase Z from Clostridium thermocellum

Hélène Souchon (1) , Silvia Spinelli (1) , Pierre Béguin (2) , Pedro M Alzari (1)

1 Immunologie structurale
2 Physiologie Cellulaire

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.

Domaines: Cristallographie; Biologie structurale [q-bio.BM]; Biochimie, Biologie Moléculaire; Bio-informatique [q-bio.QM]; Biophysique [physics.bio-ph]; Biologie cellulaire

Hélène Souchon, Silvia Spinelli, Pierre Béguin, Pedro M Alzari. Crystallization and Preliminary Diffraction Analysis of the Catalytic Domain of Xylanase Z from Clostridium thermocellum. Journal of Molecular Biology, 1994, 235 (4), pp.1348-1350. ⟨10.1006/jmbi.1994.1089⟩. ⟨pasteur-03136536⟩