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Expression, purification, crystallization and preliminary X-ray studies of the TAN1 orthologue from Methanothermobacter thermautotrophicus

DOI: 10.1107/S1744309108034039 DOI Help
PMID: 18997348 PMID Help

Authors: Ana Silva (University of Manchester) , Robert Byrne (University of York) , Maria Chechik (University of York) , Callum Smits (University of York) , David Waterman (Diamond Light Source) , Fred Antson (University of York)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 64 (11) , PAGES 1083–1086

State: Published (Approved)
Published: November 2008

Abstract: MTH909 is the Methanothermobacter thermautotrophicus orthologue of Saccharomyces cerevisiae TAN1, which is required for N4-acetylcytidine formation in tRNA. The protein consists of an N-terminal near-ferredoxin-like domain and a C-terminal THUMP domain. Unlike most other proteins containing the THUMP domain, TAN1 lacks any catalytic domains and has been proposed to form a complex with a catalytic protein that is capable of making base modifications. MTH909 has been cloned, overexpressed and purified. The molecule exists as a monomer in solution. X-ray data were collected to 2.85 Å resolution from a native crystal belonging to space group P6122 (or P6522), with unit-cell parameters a = 69.9, c = 408.5 Å.

Journal Keywords: Thump Domains; Tan1; Rna Binding

Subject Areas: Biology and Bio-materials

Facility: ESRF