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Diffraction and imaging study of imperfections of crystallized lysozyme with coherent X-raysPhase-contrast X-ray diffraction imaging and high-angular-resolution diffraction combined with phase-contrast radiographic imaging were employed to characterize defects and perfection of a uniformly grown tetragonal lysozyme crystal in the symmetric Laue case. The full-width at half-maximum (FWHM) of a 4 4 0 rocking curve measured from the original crystal was approximately 16.7 arcsec and imperfections including line defects, inclusions and other microdefects were observed in the diffraction images of the crystal. The observed line defects carry distinct dislocation features running approximately along the <1 1 0> growth front and have been found to originate mostly in a central growth area and occasionally in outer growth regions. Inclusions of impurities or formations of foreign particles in the central growth region are resolved in the images with high sensitivity to defects. Slow dehydration led to the broadening of a fairly symmetric 4 4 0 rocking curve by a factor of approximately 2.6, which was primarily attributed to the dehydration-induced microscopic effects that are clearly shown in X-ray diffraction images. The details of the observed defects and the significant change in the revealed microstructures with drying provide insight into the nature of imperfections, nucleation and growth, and the properties of protein crystals.
Document ID
20050154391
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Hu, Z. W.
(NASA Marshall Space Flight Center Huntsville, AL United States)
Chu, Y. S.
Lai, B.
Thomas, B. R.
Chernov, A. A.
Date Acquired
August 23, 2013
Publication Date
April 1, 2004
Publication Information
Publication: Acta crystallographica. Section D, Biological crystallography
Volume: 60
Issue: Pt 4
ISSN: 0907-4449
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other

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