title: Protein Crystallography at Ultra-Short Wavelengths: Feasibility Study of Anomalous-Dispersion Experiments at the Xenon K-edge.
abstract: A protein crystallography experiment at the xenon K-edge (lambda = 0.358 A) has been successfully carried out at the materials science beamline (BL2/ID11) of the ESRF. The samples used in this methodological study were crystals of porcine pancreatic elastase, a 26 kDa protein of known structure. The diffraction data are of excellent quality. The combination of isomorphous replacement and anomalous dispersion of a single xenon heavy-atom derivative allowed accurate phase determination and the computation of a high-quality electron density map of the protein molecule. This is the first fully documented report on a complete protein crystallography experiment, from data collection up to phase determination and calculation of an electron density map, carried out with data obtained at ultra-short wavelengths. Experimental considerations as well as possible advantages and drawbacks of protein crystallography at very short and ultra-short wavelengths are discussed.
authors.forename: M
authors.initials: M
authors.lastname: Schiltz
authors.forename: A
authors.initials: A
authors.lastname: Kvick
authors.forename: O S
authors.initials: OS
authors.lastname: Svensson
authors.forename: W
authors.initials: W
authors.lastname: Shepard
authors.forename: E
authors.initials: E
authors.lastname: de La Fortelle
authors.forename: T
authors.initials: T
authors.lastname: Prangé
authors.forename: R
authors.initials: R
authors.lastname: Kahn
authors.forename: G
authors.initials: G
authors.lastname: Bricogne
authors.forename: R
authors.initials: R
authors.lastname: Fourme