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Crystallographic analysis of RsmA, a ribosomal RNA small subunit methyltransferase A from Staphylococcus aureus
Yang Liu1, Yuwei Zhu1, Maikun Teng1
1Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signaling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026, People's Republic of China.
Abstract:
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 C2, 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.
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