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Crystallization and preliminary X-ray crystallographic analysis of a novel alpha-L-arabinofuranosidase (CtGH43) from Clostridium thermocellum ATCC 27405

DOI: 10.1107/S2053230X14006402 DOI Help
PMID: 24817722 PMID Help

Authors: Arun Goyal (Department of Biotechnology, Indian Institute of Technology Guwahati) , Shadab Ahmed (Department of Biotechnology, Indian Institute of Technology Guwahati) , Carlos M. G. A. Fontes (CIISA-Faculdade de Medicina Veterinaria, Universidade de Lisboa) , Shabir Najmudin (CIISA-Faculdade de Medicina Veterinaria, Universidade de Lisboa)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 70 , PAGES 616 - 618

State: Published (Approved)
Published: May 2014

Abstract: The truncated carbohydrate-active enzyme belonging to family 43 glycoside hydrolase from Clostridium thermocellum (CtGH43) is an [alpha]-L-arabinofuranosidase that in combination with endoxylanase leads to complete breakdown of L-arabinosyl-substituted xylans. The recombinant enzyme CtGH43 from C. thermocellum was overexpressed in Escherichia coli and purified by immobilized metal-ion affinity chromatography. The recombinant CtGH43 has a molecular mass of 35.86 kDa. Preliminary structural characterization was carried out on CtGH43 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 CtGH43 structure.

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

Added On: 25/02/2015 07:55

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