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Structure paper

TitleProtein Thermostabilization Requires a Fine-tuned Placement of Surface-charged Residues
Journal, issue, pagesJ. Biochem. (Tokyo), Vol. 142, Page 507-516, Year 2007
Publish dateMay 8, 2007 (structure data deposition date)
AuthorsYou, D.-J. / Fukuchi, S. / Nishikawa, K. / Koga, Y. / Takano, K. / Kanaya, S.
External linksJ. Biochem. (Tokyo) / PubMed:17761696
MethodsX-ray diffraction
Resolution2 - 2.6 Å
Structure data

PDB-2z1g:
Crystal structure of E.coli RNase HI surface charged mutant(Q4R/T40E/Q72H/Q76K/Q80E/T92K/Q105K)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2z1h:
Crystal structure of E.coli RNase HI surface charged mutant(Q4R/T92K/Q105K/Q113R/Q115K/N143K/T145K)
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-2z1i:
Crystal structure of E.coli RNase HI surface charged mutant(Q4R/T40E/Q72H/Q76K/Q80E/T92K/Q105K/Q113R/Q115K)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2z1j:
Crystal structure of E.coli RNase HI surface charged mutant(Q4R/T40E/Q72H/Q76K/Q80E/T92K/Q105K/Q113R/Q115K/N143K/T145K)
Method: X-RAY DIFFRACTION / Resolution: 2.38 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / RNase HI / thermostability / surface-charge residue

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