Macromolecular crystal data phased by negative-stained electron-microscopy reconstructions.
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.
Trapani
Stefano
S
Université de Montpellier 1, Montpellier, France. stefano.trapani@cbs.cnrs.fr
Schoehn
Guy
G
Navaza
Jorge
J
Abergel
Chantal
C
D002176:Candida albicans / Q000201:enzymology*; D018360:Crystallography, X-Ray / Q000379:methods*; D006836:Hydro-Lyases / Q000737:chemistry*; D008854:Microscopy, Electron / Q000379:methods*
D006836:Hydro-Lyases; C020000:3-dehydroquinate dehydratase