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Surface Relaxation in Protein CrystalsSurface X-ray diffraction measurements were performed on (111) growth faces of crystals of the Cellular iron-storage protein horse spleen ferritin. Crystal Trunkation Rods (CTR) were measured. A fit of the measured profile of the CTR revealed a surface roughness of 48 +/- 4.5 A and a top layer spacing contraction of 3.9 +/- 1.5%. In addition to the peak from the CTR, the rocking curves of the crystals displayed unexpected extra peaks. Multiple-scattering is demonstrated to account for them. Future applications of the method could allow the exploration of hydration effects on the growth of protein crystals.
Document ID
20030061407
Acquisition Source
Marshall Space Flight Center
Document Type
Abstract
Authors
Boutet, S. (Illinois Univ. Urbana, IL, United States)
Robinson, I. K. (Illinois Univ. Urbana, IL, United States)
Hu, Z. W. (Universities Space Research Association Huntsville, AL, United States)
Thomas, B. R. (Universities Space Research Association Huntsville, AL, United States)
Chernov, A. A. (Universities Space Research Association Huntsville, AL, United States)
Date Acquired
August 21, 2013
Publication Date
January 1, 2002
Subject Category
Nonmetallic Materials
Funding Number(s)
CONTRACT_GRANT: NCC8-66
Distribution Limits
Public
Copyright
Other

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