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Preliminary X-ray diffraction analysis of a thermophilic ?-1,3-1,4-glucanase from Clostridium thermocellum.

ABSTRACT: ?-1,3-1,4-Glucanases catalyze the specific hydrolysis of internal ?-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked ?-glucans. The thermophilic glycoside hydrolase CtGlu16A from Clostridium thermocellum exhibits superior thermal profiles, high specific activity and broad pH adaptability. Here, the catalytic domain of CtGlu16A was expressed in Escherichia coli, purified and crystallized in the trigonal space group P3121, with unit-cell parameters a=b=74.5, c=182.9?Å, by the sitting-drop vapour-diffusion method and diffracted to 1.95?Å resolution. The crystal contains two protein molecules in an asymmetric unit. Further structural determination and refinement are in progress.

SUBMITTER: Zhang L 

PROVIDER: S-EPMC4089538 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature

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Preliminary X-ray diffraction analysis of a thermophilic β-1,3-1,4-glucanase from Clostridium thermocellum.

Zhang Lilan L   Zhao Puya P   Chen Chun-Chi CC   Huang Chun-Hsiang CH   Ko Tzu-Ping TP   Zheng Yingying Y   Guo Rey-Ting RT  

Acta crystallographica. Section F, Structural biology communications 20140619 Pt 7

β-1,3-1,4-Glucanases catalyze the specific hydrolysis of internal β-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked β-glucans. The thermophilic glycoside hydrolase CtGlu16A from Clostridium thermocellum exhibits superior thermal profiles, high specific activity and broad pH adaptability. Here, the catalytic domain of CtGlu16A was expressed in Escherichia coli, purified and crystallized in the trigonal space group P3121, with unit-cell parameters a=b=74.5, c=  ...[more]

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