1. Correction of X-ray intensities from single crystals containing lattice-translocation defects
- Author
-
Andrea J. Berman, Thomas A. Steitz, Satwik Kamtekar, and Jimin Wang
- Subjects
Models, Molecular ,Diffraction ,Multiple isomorphous replacement ,Macromolecular Substances ,Protein Conformation ,Molecular Conformation ,Bacillus Phages ,DNA-Directed DNA Polymerase ,Crystal structure ,Crystallography, X-Ray ,Molecular physics ,law.invention ,X-Ray Diffraction ,Structural Biology ,law ,Lattice (order) ,Crystallization ,Models, Statistical ,Chemistry ,X-Rays ,X-ray ,General Medicine ,Crystallography ,Amplitude ,X-ray crystallography ,Software - Abstract
In 1954, Howells and colleagues described an unusual diffraction pattern from imidazole methemoglobin crystals caused by lattice-translocation defects. In these crystals, two identical lattices coexist as a single coherent mosaic block, but are translated by a fixed vector with respect to each other. The observed structure is a weighted sum of the two identical but translated structures, one from each lattice; the observed structure factors are a weighted vector sum of the two structure factors with identical unit amplitudes but shifted phases. A general procedure is described to obtain the unit amplitudes of observed structure factors from a realigned single lattice through an X-ray intensity correction. An application of this procedure is made to determine the crystal structure of phi29 DNA polymerase at 2.2 A resolution using multiple isomorphous replacement and multiwavelength anomalous dispersion methods.
- Published
- 2004