Iterative protein-model building
Lamzin, V. S.,
Perrakis, A. and
Wilson, K. S.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.8.3.1,
pp. 526-527
[ doi:10.1107/97809553602060000862 ]
Scholar
Lamzin, V. S. &
Wilson,
K. S. (1997). Automated refinement for protein crystallography. Methods Enzymol. 277, 269–305. Google Scholar
Morris, R. J., Perrakis, A. & Lamzin, V. S. (2002). ARP/wARP's model-building ...
[
more
results from section 18.8.3 in volume F]
Iterations
Lamzin, V. S.,
Perrakis, A. and
Wilson, K. S.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.8.4,
pp. 528-528
[ doi:10.1107/97809553602060000862 ]
Refinement and model building are two parts of modelling a structure
Lamzin, V. S.,
Perrakis, A. and
Wilson, K. S.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.8.1,
pp. 525-525
[ doi:10.1107/97809553602060000862 ]
are the amount of the available X-ray data (resolution) and the quality of the initial phase estimates.
References
Lamzin, V. S. &
Wilson,
K. S. (1993). Automated refinement of protein models. Acta Cryst. D 49, 129–147. Google ...
Free-atom and hybrid models
Lamzin, V. S.,
Perrakis, A. and
Wilson, K. S.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.8.2,
pp. 525-526
[ doi:10.1107/97809553602060000862 ]
Agarwal, R. C. & Isaacs, G. (1977). Method for obtaining a high resolution protein map starting from a low resolution map. Proc. Natl Acad. Sci. USA, 74, 2835–2839. Google Scholar
Lamzin, V. S. &
Wilson,
K. S. (1997). Automated ...
Refinement at atomic resolution
Dauter, Z.,
Murshudov, G. N. and
Wilson, K. S.,
International Tables for Crystallography
(2012).
Vol. F,
ch. 18.4,
pp. 485-498
[ doi:10.1107/97809553602060000858 ]
Dauter, Z. & Dauter, M. (1999). Anomalous signal of solvent bromides used for phasing of lysozyme . J. Mol. Biol. 289, 93–101. Google Scholar
Dauter, Z., Lamzin, V. S. &
Wilson,
K. S. (1997). The benefits of atomic ...
Relation to biological chemistry
Dauter, Z.,
Murshudov, G. N. and
Wilson, K. S.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.4.7,
pp. 495-496
[ doi:10.1107/97809553602060000858 ]
Restraints on coordinates and ADPs
Dauter, Z.,
Murshudov, G. N. and
Wilson, K. S.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.4.4.2,
pp. 490-490
[ doi:10.1107/97809553602060000858 ]
[
more
results from section 18.4.4 in volume F]
Deformation density
Dauter, Z.,
Murshudov, G. N. and
Wilson, K. S.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.4.5.8,
pp. 494-495
[ doi:10.1107/97809553602060000858 ]
S., Morris, R. J., Dauter, Z.,
Wilson,
K. S. & Teeter, M. M. (1999). Experimental observation of bonding electrons in proteins. J. Biol. Chem. 274, 20753–20755. Google Scholar
International Tables for Crystallography (2012 ...
[
more
results from section 18.4.5 in volume F]
Classical least-squares refinement of small molecules
Dauter, Z.,
Murshudov, G. N. and
Wilson, K. S.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.4.3.1,
pp. 488-488
[ doi:10.1107/97809553602060000858 ]
[
more
results from section 18.4.3 in volume F]
What is `atomic resolution'?
Dauter, Z.,
Murshudov, G. N. and
Wilson, K. S.,
International Tables for Crystallography
(2012).
Vol. F,
Section 18.4.1.2,
pp. 486-487
[ doi:10.1107/97809553602060000858 ]
583–601. Google Scholar
Cruickshank, D. W. J. (1999 b). Remarks about protein structure precision. Erratum . Acta Cryst. D 55, 1108. Google Scholar
Dauter, Z., Lamzin, V. S. &
Wilson,
K. S. (1997 ...
[
more
results from section 18.4.1 in volume F]
