Preparation, crystallization and preliminary X-ray diffraction analysis of PH1948, predicted RNA methyltransferase from Pyrococcus horikoshii.
- Author:
Yong-gui GAO
;
Min YAO
;
Isao TANAKA
- Publication Type:Letter
- MeSH:
Crystallization;
methods;
Molecular Conformation;
Pyrococcus horikoshii;
enzymology;
X-Ray Diffraction;
tRNA Methyltransferases;
analysis;
chemistry
- From:
Journal of Zhejiang University. Science. B
2005;6(6):454-456
- CountryChina
- Language:English
-
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 A, b=43.1 A, c=118.2 A, b=92.1 degrees , and diffract X-rays to 2.2 A resolution. The V(M) value was determined to be 2.8 A3/Da, indicating the presence of four protein molecules in the asymmetric unit.
