Structure quality and target parameters
Engh, R. A. and
Huber, R.,
International Tables for Crystallography
(2012).
Vol. F,
ch. 18.3,
pp. 474-484
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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,
pp. 483-483
[ doi:10.1107/97809553602060000857 ]
[
more
results from section 18.3.3 in volume F]
Non-bonded interactions
Engh, R. A. and
Huber, R.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.3.2.6,
pp. 482-482
[ doi:10.1107/97809553602060000857 ]
[
more
results from section 18.3.2 in volume F]
Utility of restraints: protein/special geometries
Engh, R. A. and
Huber, R.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.3.1.1,
pp. 474-474
[ doi:10.1107/97809553602060000857 ]
Opin. Struct. Biol. 7, 681–688. Google Scholar
Engh,
R. A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392–400. Google Scholar
Kleywegt, G. J ...
[
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,
pp. 483-483
[ doi:10.1107/97809553602060000857 ]
adequate computational resources and the deposition of structure factors or, even better, diffraction images.
References
Engh,
R. A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure ...
