Overexpression, crystallization and preliminary X‐ray crystallographic analysis of glucuronoxylan xylanohydrolase (Xyn30A) from Clostridium thermocellum. Issue 12 (1st December 2013)

• Record Type: Journal Article
• Authors: Verma, Anil Kumar; Goyal, Arun; Freire, Filipe; Bule, Pedro; Venditto, Immacolata; Brás, Joana L. A.; Santos, Helena; Cardoso, Vânia; Bonifácio, Cecília; Thompson, Andrew; Romão, Maria João; Prates, José A. M.; Ferreira, Luís M. A.; Fontes, Carlos M. G. A.; Najmudin, Shabir
• Is Part Of: Acta crystallographica. Volume 69:Issue 12(2013:Dec.)
• Page Start: 1440
• Page End: 1442
• Publication Date: 2013-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113025050
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The modular carbohydrate‐active enzyme belonging to glycoside hydrolase family 30 (GH30) from <italic>Clostridium thermocellum</italic> (<italic>Ct</italic>XynGH30) is a cellulosomal protein which plays an important role in plant cell‐wall degradation. The full‐length <italic>Ct</italic>XynGH30 contains an N‐terminal catalytic module (Xyn30A) followed by a family 6 carbohydrate‐binding module (CBM6) and a dockerin at the C‐terminus. The recombinant protein has a molecular mass of 45 kDa. Preliminary structural characterization was carried out on Xyn30A crystallized in different conditions. All tested crystals belonged to space group <italic>P</italic>1 with one molecule in the asymmetric unit. Molecular replacement has been used to solve the Xyn30A structure.</p> </abstract>