Characterization of dislocations in protein crystals by means of synchrotron double-crystal topography.
type: Distribution
access URL: https://hal.science/hal-00087454
format: HTML
issued: 2026-05-09T07:59:20.273969
modified: 2026-05-09T07:59:20.252380

test_moissonnage_selune
type: Agent

Characterization of dislocations in protein crystals by means of synchrotron double-crystal topography.
type: Dataset
contact point: Organization
  fn: CCSD
keyword: infoeu-reposemanticsarticle
keyword: journal-articles
keyword: x-ray-topography
keyword: crystallization
keyword: tetragonal-lysozyme
keyword: growth
keyword: radiation
keyword: diffraction
landing page: 0021-8898
description: 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.
issued: 2026-05-09T07:59:20.263551
language: en
modified: 2026-05-09T07:59:20.263556