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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/18789
Title: Characterization of dislocations in protein crystals by means of synchrotron double-crystal topography
Authors: Capelle, B.; Epelboin, Y.; Härtwig, J.; Moraleda, A. B.; Otalora, Fermín; Stojanoff, V.
Keywords: Macromolecular crystallography
Protein crystallography
Hen egg-white lysozyme
Issue Date: Feb-2004
Publisher: International Union of Crystallography
Citation: Journal of Applied Crystallography 37(1): 67-71 (2004)
Abstract: Hen egg-white lysozyme (HEWL) crystals have been studied by means of double-crystal synchrotron topography. The crystals reveal a number of features that are quite well known in hydrothermally grown inorganic crystals: dislocations, growth bands and growth sector boundaries. Dislocations in the <110> sectors have been characterized as edge dislocations with Burgers vector parallel to the c axis. They are distinguishable only under weak beam conditions. The presence of edge dislocations shown in this paper is consistent with the spiral growth steps previously reported. This spiral growth on protein crystals has been observed many times by surface techniques.
Description: 5 pages, 8 figures.
Publisher version (URL): http://dx.doi.org/10.1107/S0021889803024415
URI: http://hdl.handle.net/10261/18789
ISSN: 1067-0696
DOI: 10.1107/S0021889803024415
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