Journal of Zhejiang University SCIENCE
(ISSN 1009-3095, Monthly)

2005   Vol. 6B   No. 6   p.454-456

Preparation, crystallization and preliminary X-ray diffraction analysis of PH1948, predicted RNA methyltransferase from Pyrococcus horikoshii

GAO Yong-gui^†1,2, YAO Min¹, TANAKA Isao¹

(¹Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan)
(²School of Life Sciences, Zhejiang University, Hangzhou 310029, China)
^†E-mail: gao@castor.sci.hokudai.ac.jp
Received Mar. 25, 2005; revision accepted Apr. 10, 2005

Abstract: RNA methyltransferase is responsible for transferring methyl and resulting in methylation on the bases or ribose ring of RNA, which existed widely but mostly remains an open question. A recombinant protein PH1948 predicting RNA methyltransferase from Pyrococcus horikoshii OT3 has been crystallized. The crystals of selenomethionyl PH1948 belong to space group C2, with unit-cell parameters a=207.0 Å, b=43.1 Å, c=118.2 Å, b=92.1°, and diffract X-rays to 2.2 Å resolution. The V_M value was determined to be 2.8 ų/Da, indicating the presence of four protein molecules in the asymmetric unit.

Key words: Pyrococcus horikoshii, Methyltransferase, X-ray diffraction, Protein crystallography
doi:10.1631/jzus.2005.B0454             CLC number: Q5