Crystallization of the RNA guanylyltransferase of Chlorella virus PBCV-1 Journal Article


Authors: Doherty, A. J.; Håkansson, K.; Ho, C. K.; Shuman, S.; Wigley, D. B.
Article Title: Crystallization of the RNA guanylyltransferase of Chlorella virus PBCV-1
Abstract: RNA guanylyltransferase, or capping enzyme (E.C. 2.7.7.50) catalyzes the transfer of GMP from GTP to diphosphate-terminated RNA to form the cap structure GpppN. Chlorella virus cupping enzyme expressed in E. coli has been purified, treated with GTP and crystallized. X-ray diffraction data have been collected from these crystals as well as for a mercury derivative obtained by soaking the crystals in thimerosal. Selenomethionine RNA guanylytransferase was purified and crystallized in a similar fashion. The space group is C2221 and the cell parameters are a = 93.3, b = 214.9, c = 105.8 Å. Two Hg atoms and two subsets of Se atoms have been localized using difference Patterson and Fourier methods, suggesting that there are two molecules per asymmetric unit.
Keywords: escherichia coli; chlorella virus; paramecium bursaria chlorella virus 1
Journal Title: Acta Crystallographica Section D: Biological Crystallography
Volume: D53
Issue: 4
ISSN: 0907-4449
Publisher: Wiley Blackwell  
Date Published: 1997-07-01
Start Page: 482
End Page: 484
Language: English
DOI: 10.1107/s090744499700231x
PROVIDER: scopus
PUBMED: 15299921
DOI/URL:
Notes: Article -- Export Date: 17 March 2017 -- Source: Scopus
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  1. Chong-Kiong Ho
    33 Ho
  2. Stewart H Shuman
    546 Shuman