Published December 2002
| Version v1
Journal article
Surface relaxation in protein crystals
- 1. Department of Physics, University of Illinois, Urbana, Illinois 61801 (United States)
- 2. Universities Space Research Association, Marshall Space Flight Center, Huntsville, Alabama 35875 (United States)
Description
Surface x-ray diffraction measurements were performed on (111) growth faces of crystals of the cellular iron-storage protein, horse spleen ferritin. Crystal truncation 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
Additional details
Identifiers
Publishing Information
- Journal Title
- Physical Review. E, Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics
- Journal Volume
- 66
- Journal Issue
- 6
- Journal Page Range
- p. 061914-061914.7
- ISSN
- 1063-651X
- CODEN
- PLEEE8
INIS
- Country of Publication
- United States
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 36005193
- Subject category
- S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
- Descriptors DEI
- CONTRACTION; CRYSTAL GROWTH; CRYSTALS; FERRITIN; HORSES; HYDRATION; IRON; MULTIPLE SCATTERING; NEUTRON DIFFRACTION; RELAXATION; ROUGHNESS; SPLEEN; SURFACES; X-RAY DIFFRACTION
- Descriptors DEC
- ANIMALS; BODY; COHERENT SCATTERING; COMPLEXES; DIFFRACTION; ELEMENTS; IRON COMPLEXES; MAMMALS; METALLOPROTEINS; METALS; ORGANIC COMPOUNDS; ORGANS; PROTEINS; SCATTERING; SOLVATION; SURFACE PROPERTIES; TRANSITION ELEMENT COMPLEXES; TRANSITION ELEMENTS; VERTEBRATES
Optional Information
- Notes
- (c) 2002 The American Physical Society