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Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of the hyperthermophilic nucleotidyltransferase TTHA1015 from Thermus thermophilus HB8

Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of the... The TTHA1015 gene from Thermus thermophilus HB8 encodes a hyperthermophilic nucleotidyltransferase. TTHA1015 has high homology to proteins belonging to two related families: the nucleotidyltransferase‐domain superfamily and the DNA polymerase β‐like family. However, no crystal structures of these proteins have been reported. Determination of the crystal structure of TTHA1015 will help in elucidation of its function and will be useful for understanding the relationship between the structure and the function of these homologous proteins. In this study, TTHA1015 was expressed, purified and crystallized. X‐ray diffraction data were collected to 1.70 Å resolution. The crystal belonged to the monoclinic space group C2, with unit‐cell parameters a = 65.5, b = 34.7, c = 42.4 Å, β = 119.1°. There was one molecule per asymmetric unit, giving a Matthews coefficient of 1.86 Å3 Da−1 and an approximate solvent content of 34%. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of the hyperthermophilic nucleotidyltransferase TTHA1015 from Thermus thermophilus HB8

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References (20)

Publisher
Wiley
Copyright
International Union of Crystallography, 2011
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309111017490
pmid
21795793
Publisher site
See Article on Publisher Site

Abstract

The TTHA1015 gene from Thermus thermophilus HB8 encodes a hyperthermophilic nucleotidyltransferase. TTHA1015 has high homology to proteins belonging to two related families: the nucleotidyltransferase‐domain superfamily and the DNA polymerase β‐like family. However, no crystal structures of these proteins have been reported. Determination of the crystal structure of TTHA1015 will help in elucidation of its function and will be useful for understanding the relationship between the structure and the function of these homologous proteins. In this study, TTHA1015 was expressed, purified and crystallized. X‐ray diffraction data were collected to 1.70 Å resolution. The crystal belonged to the monoclinic space group C2, with unit‐cell parameters a = 65.5, b = 34.7, c = 42.4 Å, β = 119.1°. There was one molecule per asymmetric unit, giving a Matthews coefficient of 1.86 Å3 Da−1 and an approximate solvent content of 34%.

Journal

Acta Crystallographica Section FWiley

Published: Jul 1, 2011

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