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