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Título

Characterization of dislocations in protein crystals by means of synchrotron double-crystal topography

AutorCapelle, B.; Epelboin, Y.; Härtwig, J.; Moraleda, A. B.; Otalora, Fermín; Stojanoff, V.
Palabras claveMacromolecular crystallography
Protein crystallography
Hen egg-white lysozyme
Topography
Dislocations
Fecha de publicaciónfeb-2004
EditorInternational Union of Crystallography
CitaciónJournal of Applied Crystallography 37(1): 67-71 (2004)
ResumenHen 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.
Descripción5 pages, 8 figures.
Versión del editorhttp://dx.doi.org/10.1107/S0021889803024415
URIhttp://hdl.handle.net/10261/18789
DOI10.1107/S0021889803024415
ISSN1067-0696
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