Science Letters:Preparation, crystallization and preliminary X-ray diffraction analysis of PH1948, predicted RNA methyltransferase from Pyrococcus horikoshii
- Author:
Yong-Gui GAO
1
;
Min YAO
;
Isao TANAKA
Author Information
1. Hokkaido University
- Keywords:
Pyrococcus horikoshii;
Methyltransferase;
X-ray diffraction;
Protein crystallography
- From:
Journal of Zhejiang University. Science. B
2005;6(6):454-456
- CountryChina
- Language:Chinese
-
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), β=92.1°, and diffract X-rays to 2.2(A) resolution. The VM value was determined to be 2.8(A)3/Da, indicating the presence of four protein molecules in the asymmetric unit.
