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 Results for DC.creator="R." AND DC.creator="A." AND DC.creator="Engh" in section 18.3.1 of 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 ( ...

Utility of restraints: protein/special geometries
Engh, R. A. and Huber, R.  International Tables for Crystallography (2012). Vol. F, Section 18.3.1.1, p. 474 [ doi:10.1107/97809553602060000857 ]
... from the CSD have come into widespread use for protein (Engh & Huber, 1991; Brünger, 1993; Priestle, 1994) and nucleic acid ... and data collection and processing remain. On the other hand, a structure with an unusual chemical environment might require a tailored parameterization scheme to study the effects of this ...

Purpose of restraints
Engh, R. A. and Huber, R.  International Tables for Crystallography (2012). Vol. F, Section 18.3.1, p. 474 [ doi:10.1107/97809553602060000857 ]
... 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 an accurate model for X-ray scattering, calculate a measurement-time-averaged electron-density distribution for that structure ...

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