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Structure paper

TitleImprovement of crystal quality by surface mutations of beta-lactamase Toho-1
Journal, issue, pagesActa Crystallogr. ,Sect. F, Vol. 65, Page 379-382, Year 2009
Publish dateAug 7, 2008 (structure data deposition date)
AuthorsShimamura, T. / Nitanai, Y. / Uchiyama, T. / Matsuzawa, H.
External linksActa Crystallogr. ,Sect. F / PubMed:19342785
MethodsX-ray diffraction
Resolution1.03 Å
Structure data

PDB-2zq8:
Apo structure of class a beta-lactamase Toho-1 R274N/R276N double mutant
Method: X-RAY DIFFRACTION / Resolution: 1.03 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / EXTENDED-SPECTRUM / ESBL / BETA-LACTAMASE / TOHO-1 / Antibiotic resistance / Plasmid

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