<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>64(Pt 12)</volume><submitter>Priyadarshi A</submitter><pubmed_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 A 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 A, 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 A(3) Da(-1) and a solvent content of 50%.</pubmed_abstract><journal>Acta crystallographica. Section F, Structural biology and crystallization communications</journal><pagination>1166-8</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2593692</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Crystallization and preliminary X-ray crystallographic analysis of the probable tRNA-modification GTPase (TrmE) from Staphylococcus aureus.</pubmed_title><pmcid>PMC2593692</pmcid><pubmed_authors>Priyadarshi A</pubmed_authors><pubmed_authors>Nam KH</pubmed_authors><pubmed_authors>Kim EE</pubmed_authors><pubmed_authors>Hwang KY</pubmed_authors></additional><is_claimable>false</is_claimable><name>Crystallization and preliminary X-ray crystallographic analysis of the probable tRNA-modification GTPase (TrmE) from Staphylococcus aureus.</name><description>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 A 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 A, 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 A(3) Da(-1) and a solvent content of 50%.</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Dec</publication><modification>2024-11-13T19:54:15.753Z</modification><creation>2019-03-27T00:00:45Z</creation></dates><accession>S-EPMC2593692</accession><cross_references><pubmed>19052377</pubmed><doi>10.1107/s1744309108036579</doi><doi>10.1107/S1744309108036579</doi></cross_references></HashMap>