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Cloning, purification, crystallization and preliminary crystallographic analysis of the human histone deacetylase sirtuin 1

DOI: 10.1107/S1744309111003277 DOI Help
PMID: 21505241 PMID Help

Authors: Kenneth Holbourn (University of Bath) , Matthew Lloyd (University of Bath) , Andrew Thompson (University of Bath) , Michael Threadgill (University of Bath) , Ravi Acharya (University of Bath)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 67 (4) , PAGES 461-463

State: Published (Approved)
Published: April 2011

Abstract: Human sirtuin 1 is a member of the histone deacetylase family and is involved in cellular aging, tumourigenesis and cellular metabolism. Recombinant sirtuin 1 comprising residues 140-747 was crystallized using the hanging-drop vapour-diffusion method. The crystal diffracted to 3.4 Å resolution and belonged to space group P622, with unit-cell parameters a = b = 203.1, c = 625.3 Å, and is estimated to contain between six and 12 molecules per asymmetric unit.

Journal Keywords: Sirtuin 1; Histone Deacetylases

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography

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