Priyadarshi, Amit Nam, Ki Hyun Kim, Eunice EunKyeong Hwang, Kwang Yeon 2024-01-20T22:30:25Z 2024-01-20T22:30:25Z 2021-08-31 2008-12 2053-230X https://pubs.kist.re.kr/handle/201004/132968 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%. English INT UNION CRYSTALLOGRAPHY COLI MNME PROTEIN Crystallization and preliminary X-ray crystallographic analysis of the probable tRNA-modification GTPase (TrmE) from Staphylococcus aureus Article 10.1107/S1744309108036579 1 ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.64, pp.1166 - 1168 ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS 64 1166 1168 scie scopus 000261198700022 2-s2.0-57349089828 Biochemical Research Methods Biochemistry & Molecular Biology Biophysics Crystallography Biochemistry & Molecular Biology Biophysics Crystallography Article COLI MNME PROTEIN GDP GTP GTPases Probable tRNA modification Staphylococcus aureus TrmE