Studying protein–ligand interactions using x-ray crystallography

Turnbull, Andrew P. and Emsley, P. (2013) Studying protein–ligand interactions using x-ray crystallography. In: Williams, Mark A. and Daviter, Tina (eds.) Protein–Ligand Interactions: Fundamentals. Methods in Molecular Biology VI 1008. Berlin, Germany: Springer, pp. 457-477. ISBN 9781627033978.

Full text not available from this repository.

Official URL: http://dx.doi.org/10.1007/978-1-62703-398-5_17

Abstract

X-ray crystallography is a powerful technique for studying protein–ligand interactions. Advances in techniques have meant that it is now possible to routinely determine the structures of ligand complexes in the majority of cases where crystallization conditions and protein structures are already known. Ligand soaking or cocrystallization, together with the potential use of molecular replacement, provides data for determining the structures of a protein in complex with ligands. Furthermore, advances in protein structure model building facilitate automatic ligand fitting to residual electron density in the protein–ligand complex.

Metadata

Item Type:	Book Section
Additional Information:	Series ISSN: 1064-3745
Keyword(s) / Subject(s):	X-ray crystallography, Crystallization, Molecular replacement, Ligand fitting, COOT
School:	Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
Depositing User:	Administrator
Date Deposited:	29 Jan 2014 13:41
Last Modified:	02 Aug 2023 17:09
URI:	https://eprints.bbk.ac.uk/id/eprint/9112

Statistics

Archive Staff Only (login required)

Edit/View Item