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Assessing the quality of macromolecular structures
Wodak, S. J., Vagin, A. A., Richelle, J., Das, U., Pontius, J. and Berman, H. M.  International Tables for Crystallography (2012). Vol. F, ch. 21.2, pp. 662-676 [ doi:10.1107/97809553602060000880 ]
... 104 nucleic acid crystal structures considered in the study of Das et al. (2001): (a) correlation coefficient, (b) maximal error, (c ... A. Ralph & S. Bailey, pp. 11-22. Warrington: Daresbury Laboratory. Das, U., Chen, S., Fuxreiter, M., Vaguine, A. A., Richelle, J., ...

Atomic resolution structures
Wodak, S. J., Vagin, A. A., Richelle, J., Das, U., Pontius, J. and Berman, H. M.  International Tables for Crystallography (2012). Vol. F, Section 21.2.4, p. 673 [ doi:10.1107/97809553602060000880 ]
Atomic resolution structures 21.2.4. Atomic resolution structures With improved techniques of crystallization and data collection using synchrotron radiation and cryogenic cooling, an increasing number of protein crystal structures are being determined at atomic resolution (1.2 or better). With atomic resolution data, refinement can be performed that requires much less strict ...

Assessing the quality in specific regions of a model
Wodak, S. J., Vagin, A. A., Richelle, J., Das, U., Pontius, J. and Berman, H. M.  International Tables for Crystallography (2012). Vol. F, Section 21.2.3.1.3.2, pp. 670-673 [ doi:10.1107/97809553602060000880 ]
Assessing the quality in specific regions of a model 21.2.3.1.3.2. Assessing the quality in specific regions of a model The main purpose for computing the four local quality measures, the B factor, the Density index, the atomic displacement (Shift) and the Density correlation (Table 21.2.3.3), is to identify problem regions in ...
     [more results from section 21.2.3 in volume F]

Deviations from standard atomic volumes as a quality measure for protein crystal structures
Wodak, S. J., Vagin, A. A., Richelle, J., Das, U., Pontius, J. and Berman, H. M.  International Tables for Crystallography (2012). Vol. F, Section 21.2.2.2.3, pp. 664-665 [ doi:10.1107/97809553602060000880 ]
Deviations from standard atomic volumes as a quality measure for protein crystal structures 21.2.2.2.3. Deviations from standard atomic volumes as a quality measure for protein crystal structures The observations that protein X-ray structures are at least as tightly packed as small-molecule crystals (Richards, 1974; Harpaz et al., 1994) and ...
     [more results from section 21.2.2 in volume F]

Introduction
Wodak, S. J., Vagin, A. A., Richelle, J., Das, U., Pontius, J. and Berman, H. M.  International Tables for Crystallography (2012). Vol. F, Section 21.2.1, p. 662 [ doi:10.1107/97809553602060000880 ]
Introduction 21.2.1. Introduction X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy are the two major techniques that provide detailed information on the atomic structure of macromolecules. Usually, however, the data obtained from these techniques are not of high enough resolution to define the atomic positions of a macromolecule with sufficient ...

Concluding remarks
Wodak, S. J., Vagin, A. A., Richelle, J., Das, U., Pontius, J. and Berman, H. M.  International Tables for Crystallography (2012). Vol. F, Section 21.2.5, p. 673 [ doi:10.1107/97809553602060000880 ]
... A. Ralph & S. Bailey, pp. 11-22. Warrington: Daresbury Laboratory. Das, U., Chen, S., Fuxreiter, M., Vaguine, A. A., Richelle, J., Berman ...

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