Crystallization of the catalytic domain of Clostridium cellulolyticum CeLF cellulase in the presence of a newly synthesized cellulase inhibitor.
The catalytic domain of the CeIF processive endocellulase, a family 48 glycosyl hydrolase from Clostridium cellulolyticum has been crystallized in the presence of a newly synthesized inhibitor (methyl 4-S-beta-cellobiosyl-4-thio-beta-cellobioside), by vapour diffusion, using PEG as a precipitant. The protein crystallizes in the orthorhombic P212121 space group and diffracts to a resolution of 2.0 A. The unit-cell parameters are a = 61.4, b = 84.5, c = 121.9 A.
Université de Provence, Place Victor-Hugo, 13331 Marseille CEDEX 3, France.
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Reverbel-Leroy
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Parsiegla
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Moreau
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Juy
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Tardif
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Driguez
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Bélaich
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Haser
D002240:Carbohydrate Sequence; D020134:Catalytic Domain; D002480:Cellulase / Q000032:analysis* / Q000737:chemistry*; D003013:Clostridium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009844:Oligosaccharides / Q000737:chemistry*
D004791:Enzyme Inhibitors; D009844:Oligosaccharides; C115614:methyl 4-cellobiosyl-4-thiocellobioside; D002480:Cellulase