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Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):67-74. Epub 2004 Dec 17.

Correction of X-ray intensities from single crystals containing lattice-translocation defects.

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520-8114, USA. wang@mail.csb.yale.edu

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.

PMID:
15608377
DOI:
10.1107/S0907444904026721
[Indexed for MEDLINE]

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