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Structure paper

TitleProtein core adaptability: crystal structures of the cavity-filling variants of Escherichia coli RNase HI
Journal, issue, pagesProtein Pept. Lett., Vol. 17, Page 1163-1169, Year 2010
Publish dateNov 11, 2009 (structure data deposition date)
AuthorsTanaka, M. / Chon, H. / Angkawidjaja, C. / Koga, Y. / Takano, K. / Kanaya, S.
External linksProtein Pept. Lett. / PubMed:20423323
MethodsX-ray diffraction
Resolution1.79 - 2.2 Å
Structure data

PDB-3aa2:
A52I E. coli RNase HI
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3aa3:
A52L E. coli RNase HI
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3aa4:
A52V E.coli RNase HI
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

PDB-3aa5:
A52F E.coli RNase HI
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / stability / cavity / Endonuclease / Magnesium / Metal-binding / Nuclease

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