J. Appl. Cryst. (2000). 33, 958-963 [ doi:10.1107/S0021889800004441 ]
Abstract: The FBR (Fourier basis reconstruction) method described in this paper has been designed to determine the basis matrix of the Bravais lattice with respect to the laboratory frame of reference and without prior knowledge of cell constants, particularly for protein crystals of comparatively low quality. It is based on Fourier analysis of a three-dimensional intensity distribution in reciprocal space, which is directly obtained from observed intensity distributions, provided that they are recorded by the rotation method using a fixed X-ray wavelength, resulting in a direct-space determination of the basis vectors. After a description of the motivation and theory behind the method, it is tested by application to numerically generated images of a virtual sample crystal and to experimental data of a lysozyme crystal with well known cell constants. Finally, FBR is applied to a set of images of bacteriorhodopsin crystals suffering from strong anisotropic spot broadening; this case provided the original motivation for the present work.
Copyright © International Union of Crystallography
IUCr Webmaster