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TitleMacromolecular crystal data phased by negative-stained electron-microscopy reconstructions.
Journal, issue, pagesActa Crystallogr D Biol Crystallogr, Vol. 66, Issue Pt 5, Page 514-521, Year 2010
Publish dateApr 21, 2010
AuthorsStefano Trapani / Guy Schoehn / Jorge Navaza / Chantal Abergel /
PubMed AbstractThe combination of transmission electron microscopy with X-ray diffraction data is usually limited to relatively large particles. Here, the approach is continued one step further by utilizing ...The combination of transmission electron microscopy with X-ray diffraction data is usually limited to relatively large particles. Here, the approach is continued one step further by utilizing negative staining, a technique that is of wider applicability than cryo-electron microscopy, to produce models of medium-size proteins suitable for molecular replacement. The technique was used to solve the crystal structure of the dodecameric type II dehydroquinase enzyme from Candida albicans (approximately 190 kDa) and that of the orthologous Streptomyces coelicolor protein.
External linksActa Crystallogr D Biol Crystallogr / PubMed:20445226
MethodsEM (single particle) / X-ray diffraction
Resolution2.95 - 15.0 Å
Structure data

EMDB-1680:
Macromolecular crystal data phased by negative staining electron microscopy reconstructions
Method: EM (single particle) / Resolution: 15.0 Å

PDB-3kip:
Crystal structure of type-II 3-dehydroquinase from C. albicans
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM / Tris

ChemComp-HOH:
WATER / Water

Source
  • candida albicans (yeast)
KeywordsLYASE

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