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Characterization of dislocations in protein crystals by means of synchrotron double‐crystal topography
Author(s) -
Capelle B.,
Epelboin Y.,
Härtwig J.,
Moraleda A. B.,
Otálora F.,
Stojanoff V.
Publication year - 2004
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889803024415
Subject(s) - burgers vector , crystallography , synchrotron , materials science , crystal (programming language) , dislocation , enhanced data rates for gsm evolution , crystal growth , spiral (railway) , protein crystallization , condensed matter physics , characterization (materials science) , chemical physics , optics , chemistry , crystallization , nanotechnology , physics , telecommunications , mathematical analysis , programming language , mathematics , organic chemistry , computer science
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.