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Crystallization and preliminary X‐ray crystallographic analysis of a novel α‐L‐arabinofuranosidase ( Ct GH43) from Clostridium thermocellum ATCC 27405
Author(s) -
Goyal Arun,
Ahmed Shadab,
Fontes Carlos M. G. A.,
Najmudin Shabir
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14006402
Subject(s) - clostridium thermocellum , crystallization , chemistry , clostridium , crystallography , biochemistry , bacteria , enzyme , biology , cellulase , organic chemistry , genetics
The truncated carbohydrate‐active enzyme belonging to family 43 glycoside hydrolase from Clostridium thermocellum ( Ct GH43) is an α‐L‐arabinofuranosidase that in combination with endoxylanase leads to complete breakdown of L‐arabinosyl‐substituted xylans. The recombinant enzyme Ct GH43 from C. thermocellum was overexpressed in Escherichia coli and purified by immobilized metal‐ion affinity chromatography. The recombinant Ct GH43 has a molecular mass of 35.86 kDa. Preliminary structural characterization was carried out on Ct GH43 crystallized from different conditions, which gave either cube‐shaped or brick‐shaped crystals. These diffracted to a resolution of 1.65 Å for the cubic form and 1.1 Å for the monoclinic form. Molecular replacement was used to solve the Ct GH43 structure.