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Crystallographic analysis of RsmA, a ribosomal RNA small subunit methyltransferase A from Staphylococcus aureus
Author(s) -
Liu Yang,
Zhu Yuwei,
Teng Maikun,
Li Xu
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15011279
Subject(s) - staphylococcus aureus , ribosomal rna , methyltransferase , protein subunit , methylation , chemistry , microbiology and biotechnology , biology , crystallography , biochemistry , dna , genetics , bacteria , gene
RsmA, a ribosomal RNA small subunit methyltransferase from Staphylococcus aureus , catalyzes the N 6 methylation of adenine in 16S rRNA. In this study, RsmA from Staphylococcus aureus was cloned, expressed, purified and crystallized. The crystal belonged to space group C 2, with unit‐cell parameters a = 84.38, b = 157.76, c = 96.50 Å, β = 95.04°. X‐ray diffraction data were collected to a resolution of 3.2 Å. The self‐rotation function and the Matthews coefficient suggested the presence of two molecules in the asymmetric unit.