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Structure quality and target parameters
Engh, R. A. and Huber, R.  International Tables for Crystallography (2012). Vol. F, ch. 18.3, pp. 474-484 [ doi:10.1107/97809553602060000857 ]
... and angles derived from atomic resolution structures. This article describes a set of bond and angle target parameters derived from small ... see, are two materially different laws. (Adapted from William James.) A wise man, therefore, proportions his restraints to the evidence. (Adapted ... complex diffuse scattering function of an X-ray beam from a single macromolecular structure to arbitrary resolution, we could, given ...

Confidence in restraints versus information from diffraction
Engh, R. A. and Huber, R.  International Tables for Crystallography (2012). Vol. F, Section 18.3.3.1, p. 483 [ doi:10.1107/97809553602060000857 ]
Confidence in restraints versus information from diffraction 18.3.3.1. Confidence in restraints versus information from diffraction Primarily in cases of new structures, such as small-ligand- or metal-binding proteins, the refinement may indicate that the expected geometries and applied restraints seem incompatible with evidence from the electron density. Several sources for ...
     [more results from section 18.3.3 in volume F]

Addition of tailored information sources
Engh, R. A. and Huber, R.  International Tables for Crystallography (2012). Vol. F, Section 18.3.2.9, p. 483 [ doi:10.1107/97809553602060000857 ]
... encoded by the refinement program, it is for most programs a simple matter to introduce new atom types, residues, or fragment ...
     [more results from section 18.3.2 in volume F]

Risk of restraints: bias, lack of cross validation
Engh, R. A. and Huber, R.  International Tables for Crystallography (2012). Vol. F, Section 18.3.1.2, p. 474 [ doi:10.1107/97809553602060000857 ]
... available for such cross validation. For example, the use of a force field in protein refinement that strictly enforces a physical distribution of the protein backbone [varphi]-[psi] angles of ... error-induced strain into other degrees of freedom while eliminating a Ramachandran analysis as a tool for judging protein quality ( ...
     [more results from section 18.3.1 in volume F]

Future perspectives
Engh, R. A. and Huber, R.  International Tables for Crystallography (2012). Vol. F, Section 18.3.4, p. 483 [ doi:10.1107/97809553602060000857 ]
... the best (most accurate) possible parameterization and establish it as a standard (to enable statistical structure comparisons). This does not seem to be a realistic goal for several reasons. Firstly, the parameterization is less a determinant of accuracy than the quality of the data ...

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