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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt 1):90-2. Epub 2004 Dec 2.

Expression, purification, crystallization and preliminary crystallographic study of a potential metal-dependent hydrolase with cyclase activity from Thermoanaerobacter tengcongensis.

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1
State Key Laboratory for Structural Chemistry of Unstable and Stable Species, College of Chemistry, Peking University, Beijing 100871, People's Republic of China.

Abstract

The putative metal-dependent hydrolase gene TTE1006 from Thermoanaerobacter tengcongensis strain MB4T (T = type strain; Genbank accession No. AE008691) was heterologously expressed in Escherichia coli. The 205-amino-acid gene product was purified and crystallized. The crystal used for data collection belongs to space group P2(1), with unit-cell parameters a = 85.2, b = 62.1, c = 172.4 A, beta = 104.2 degrees. Using a synchrotron-radiation source, the resolution limit of the data reached 1.87 A. Eight molecules were estimated to be present in the asymmetric unit, with a solvent content of 48%. Structure determination is ongoing using the multiple-wavelength anomalous diffraction (MAD) method and also the molecular-replacement (MR) method.

PMID:
16508100
PMCID:
PMC1952373
DOI:
10.1107/S1744309104029392
[Indexed for MEDLINE]
Free PMC Article
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