Multipattern Rietveld refinement of protein powder data : an approach to higher resolution.
Journal Article
·
· J. Appl. Crystallogr.
By using combinations of multiple protein powder diffraction patterns obtained from an image plate to a d-spacing of 2 {angstrom}, which differ by solvent-induced and radiation-damage-induced lattice strains, the powder overlap problem is partially resolved in a stereochemically restrained Rietveld refinement. The results for hen egg white lysozyme (HEWL) include, for the first time with powder data, placement of a substantial number of water molecules and structural results that approach the quality normally obtained by single-crystal methods. This study explores the lattice strains induced by changes in salt concentration, changes in solvent pH and the effect of low-dose radiation damage. For HEWL, lattice strains are not monotonic, so that with increasing NaCl concentration (0.25-1.25 M) the a axis increases by {approx}0.5%, while the c axis decreases by {approx}1.5%, and this variation is pH dependent. Low-dose radiation damage similarly induces non-monotonic lattice strains, similar but smaller than those arising from increased salt concentration. The effect of using these powder data in a combined Rietveld analysis is effectively to deconvolute the overlapping reflections by differing shifts in their relative positions.
- Research Organization:
- Argonne National Laboratory (ANL)
- Sponsoring Organization:
- SC
- DOE Contract Number:
- AC02-06CH11357
- OSTI ID:
- 945250
- Report Number(s):
- ANL/XSD/JA-57779
- Journal Information:
- J. Appl. Crystallogr., Journal Name: J. Appl. Crystallogr. Journal Issue: 2007 Vol. 40; ISSN JACGAR; ISSN 0021-8898
- Country of Publication:
- United States
- Language:
- ENGLISH
Similar Records
High-pressure protein crystallography of hen egg-white lysozyme
On the possibility of using polycrystalline material in the development of structure-based generic assays
ATP-induced noncooperative thermal unfolding of hen lysozyme
Journal Article
·
Wed Apr 01 00:00:00 EDT 2015
· Acta Crystallographica. Section D: Biological Crystallography
·
OSTI ID:22347698
On the possibility of using polycrystalline material in the development of structure-based generic assays
Journal Article
·
Wed Apr 01 00:00:00 EDT 2009
· Acta Crystallographica. Section D: Biological Crystallography
·
OSTI ID:22347976
ATP-induced noncooperative thermal unfolding of hen lysozyme
Journal Article
·
Fri Jul 02 00:00:00 EDT 2010
· Biochemical and Biophysical Research Communications
·
OSTI ID:22202678