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 methyl-transferase 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, β=92.1°, and diffract X-rays to 2.2 Å resolution. The VM value was determined to be 2.8 Å3/Da, indicating the presence of four protein molecules in the asymmetric unit.
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Project supported by the National Project on Protein Structural and Functional Analyses from the Ministry of Education, Culture, Sports, Science, and Technology of Japan
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Gao, Yg., Yao, M. & Tanaka, I. Preparation, crystallization and preliminary X-ray diffraction analysis of PH1948, predicted RNA methyltransferase from Pyrococcus horikoshii. J Zheijang Univ Sci B 6, 454–456 (2005). https://doi.org/10.1631/jzus.2005.B0454
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DOI: https://doi.org/10.1631/jzus.2005.B0454