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Crystallization and preliminary X-ray crystallographic analysis of the probable tRNA-modification GTPase (TrmE) from Staphylococcus aureus

Authors
Priyadarshi, AmitNam, Ki HyunKim, Eunice EunKyeongHwang, Kwang Yeon
Issue Date
12월-2008
Publisher
INT UNION CRYSTALLOGRAPHY
Keywords
GDP; GTP; GTPases; Probable tRNA modification; Staphylococcus aureus; TrmE
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.64, pp.1166 - 1168
Indexed
SCIE
SCOPUS
Journal Title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume
64
Start Page
1166
End Page
1168
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/122282
DOI
10.1107/S1744309108036579
ISSN
2053-230X
Abstract
Probable tRNA-modification GTPase (TrmE) is a guanine nucleotide-binding protein that is conserved between bacteria and humans. GTPase hydrolyzes GTP and plays a pivotal role in signalling pathways. In this study, TrmE from Staphylococcus aureus was overexpressed in Escherichia coli. The enzyme was found to crystallize at 295 K when ammonium sulfate was used as a precipitant. X-ray diffraction data were collected to 2.9 angstrom resolution from the crystallized enzyme using synchrotron radiation. The crystal was found to belong to the cubic space group I23, with unit-cell parameters a = b = c = 229.47 angstrom, alpha = beta = gamma = 90 degrees. The crystal is likely to contain four monomers in the asymmetric unit, with a corresponding V-M of 2.4 angstrom 3 Da(-1) and a solvent content of 50%.
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