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Schiltz M, Kvick A, Svensson OS, et al. Protein Crystallography at Ultra-Short Wavelengths: Feasibility Study of Anomalous-Dispersion Experiments at the Xenon K-edge. J Synchrotron Radiat. 1997;4:287-97doi: 10.1107/S0909049597008571.
Schiltz, M., Kvick, A., Svensson, O. S., Shepard, W., de La Fortelle, E., Prangé, T., Kahn, R., Bricogne, G., & Fourme, R. (1997). Protein Crystallography at Ultra-Short Wavelengths: Feasibility Study of Anomalous-Dispersion Experiments at the Xenon K-edge. Journal of synchrotron radiation, 4287-97. https://doi.org/10.1107/S0909049597008571
Schiltz, M, et al. "Protein Crystallography at Ultra-Short Wavelengths: Feasibility Study of Anomalous-Dispersion Experiments at the Xenon K-edge." Journal of synchrotron radiation vol. 4 (1997): 287-97. doi: https://doi.org/10.1107/S0909049597008571
Schiltz M, Kvick A, Svensson OS, Shepard W, de La Fortelle E, Prangé T, Kahn R, Bricogne G, Fourme R. Protein Crystallography at Ultra-Short Wavelengths: Feasibility Study of Anomalous-Dispersion Experiments at the Xenon K-edge. J Synchrotron Radiat. 1997 Sep 01;4:287-97. doi: 10.1107/S0909049597008571. PMID: 16699242.
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J Synchrotron Radiat. 1997 Sep 01;4:287-97. doi: 10.1107/S0909049597008571.

Protein Crystallography at Ultra-Short Wavelengths: Feasibility Study of Anomalous-Dispersion Experiments at the Xenon K-edge.

Journal of synchrotron radiation

M Schiltz, A Kvick, O S Svensson, W Shepard, E de La Fortelle, T Prangé, R Kahn, G Bricogne, R Fourme

PMID: 16699242 DOI: 10.1107/S0909049597008571

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.

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