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