Advances in direct methods for protein crystallography

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Advances in direct methods for protein crystallography.

Recent advances in ab initio direct methods have enabled the solution of crystal structures of small proteins from native X-ray data alone, that is, without the use of fragments of known structure or the need to prepare heavy-atom or selenomethionine derivatives, provided that the data are available to atomic resolution. These methods are also proving to be useful for locating the selenium atom...

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In the most developed branches of crystallography, structure solution proceeds by two distinct steps: first, an approximate model of the structure is deduced directly from the measured data by an algorithm which assumes no preconceived model; second, a process of structure refinement simulates the experimental data for systematic variations of the parameters of such a model and determines a fin...

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Direct methods and protein crystallography at low resolution.

The tools of modern direct methods are examined and their limitations for solving protein structures discussed. Direct methods need atomic resolution data (1.1-1.2 A) for structures of around 1000 atoms if no heavy atom is present. For low-resolution data, alternative approaches are necessary and these include maximum entropy, symbolic addition, Sayre's equation, group scattering factors and el...

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Apotheosis, not apocalypse: methods in protein crystallography.

European Molecular Biology Laboratory, Hamburg Outstation, c/o DESY, Notkestrasse 85, 22603 Hamburg, Germany, European Molecular Biology Laboratory, Grenoble Outstation, c/o ILL, BP 156, 6 Rue Jules Horowitz, 38043 Grenoble CEDEX 9, France, MRC Laboratory for Molecular Biology, Hills Road, Cambridge, England, Biology Department, Brookhaven National Laboratory, Upton NY 11973-5000, USA, and Depa...

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Direct Methods of Structure Analysis in Polymer Crystallography

The use of direct phasing techniques, of the type familiar to small molecule x-ray crystallographers, for solving polymer crystal structures is discussed. Single crystal intensities from electron diffraction experiments are particularly useful, especially if the complete reciprocal lattice can be sampled. Furthermore, the analysis of powder or fiber x-ray data also is not precluded, especially ...

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ژورنال

عنوان ژورنال: Current Opinion in Structural Biology

سال: 1999

ISSN: 0959-440X

DOI: 10.1016/s0959-440x(99)00020-2