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Crystallization and preliminary X-ray crystallographic analysis of the probable tRNA-modification GTPase (TrmE) from Staphylococcus aureus.
- Source :
-
Acta Crystallographica: Section F (Wiley-Blackwell) . Dec2008, Vol. 64 Issue 12, p1166-1168. 3p. - Publication Year :
- 2008
-
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 Å 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 Å, α = β = γ = 90°. The crystal is likely to contain four monomers in the asymmetric unit, with a corresponding VM of 2.4 Å3 Da−1 and a solvent content of 50%. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 64
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 110812066
- Full Text :
- https://doi.org/10.1107/S1744309108036579