Preparation, crystallization and preliminary X-ray diffraction analysis of PH1948, predicted RNA methyltransferase from Pyrococcus horikoshii.
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.
Gao
Yong-gui
YG
Yao
Min
M
Tanaka
Isao
I
D003460:Crystallization / Q000379:methods*; D008968:Molecular Conformation; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D014961:X-Ray Diffraction; D012359:tRNA Methyltransferases / Q000032:analysis* / Q000737:chemistry*
D012359:tRNA Methyltransferases