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Structure paper

TitleStructures of Two Highly Homologous Bacterial L-Asparaginases: A Case of Enantiomorphic Space Groups
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 57, Page 369-, Year 2001
Publish dateDec 5, 2000 (structure data deposition date)
AuthorsJaskolski, M. / Kozak, M. / Lubkowski, J. / Palm, G.J. / Wlodawer, A.
External linksActa Crystallogr. ,Sect. D / PubMed:11223513
MethodsX-ray diffraction
Resolution2.17 - 2.5 Å
Structure data

PDB-1hfj:
Asparaginase from Erwinia chrysanthemi, hexagonal form with sulfate
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1hfk:
Asparaginase from Erwinia chrysanthemi, hexagonal form with weak sulfate
Method: X-RAY DIFFRACTION / Resolution: 2.17 Å

PDB-1ho3:
CRYSTAL STRUCTURE ANALYSIS OF E. COLI L-ASPARAGINASE II (Y25F MUTANT)
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-ASP:
ASPARTIC ACID

Source
  • erwinia chrysanthemi (bacteria)
  • escherichia coli (E. coli)
KeywordsHYDROLASE / asparaginase / leukemia

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