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Received: 2005-03-25
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Preparation, crystallization and preliminary X-ray diffraction analysis of PH1948, predicted RNA methyltransferase from Pyrococcus horikoshii
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GAO Yong-gui, YAO Min, TANAKA Isao. Preparation, crystallization and preliminary X-ray diffraction analysis of PH1948, predicted RNA methyltransferase from Pyrococcus horikoshii[J]. Journal of Zhejiang University Science B, 2005, 6(6): 454-456.
@article{title="Preparation, crystallization and preliminary X-ray diffraction analysis of PH1948, predicted RNA methyltransferase from Pyrococcus horikoshii",
author="GAO Yong-gui, YAO Min, TANAKA Isao",
journal="Journal of Zhejiang University Science B",
volume="6",
number="6",
pages="454-456",
year="2005",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.2005.B0454"
}
%0 Journal Article
%T Preparation, crystallization and preliminary X-ray diffraction analysis of PH1948, predicted RNA methyltransferase from Pyrococcus horikoshii
%A GAO Yong-gui
%A YAO Min
%A TANAKA Isao
%J Journal of Zhejiang University SCIENCE B
%V 6
%N 6
%P 454-456
%@ 1673-1581
%D 2005
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2005.B0454
TY - JOUR
T1 - Preparation, crystallization and preliminary X-ray diffraction analysis of PH1948, predicted RNA methyltransferase from Pyrococcus horikoshii
A1 - GAO Yong-gui
A1 - YAO Min
A1 - TANAKA Isao
J0 - Journal of Zhejiang University Science B
VL - 6
IS - 6
SP - 454
EP - 456
%@ 1673-1581
Y1 - 2005
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.2005.B0454
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 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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