Crystallization and Preliminary Diffraction Analysis of the Catalytic Domain of Xylanase Z from Clostridium thermocellum - Archive ouverte HAL Access content directly
Journal Articles Journal of Molecular Biology Year : 1994

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

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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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pasteur-03136536 , version 1 (09-02-2021)

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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⟩

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