1. Crystallization of protein-ligand complexes
- Author
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Robert X. Xu, Lisa M. Shewchuk, Robert T. Gampe, Tamara E. Grisard, Shawn P. Williams, Gang An, Liping Wang, Su-Jun J. Deng, Warren J. Rocque, Anne M. Hassell, Robert T. Nolte, Kurt Weaver, Kevin P. Madauss, H. Luke Carter, Jane Bynum, G. Bruce Wisely, and Randy K. Bledsoe
- Subjects
crystallization ,Stereochemistry ,Ab initio ,Molecular Conformation ,Crystallography, X-Ray ,Ligands ,Cofactor ,Receptors, Glucocorticoid ,Structural Biology ,Protein purification ,Molecule ,Animals ,Humans ,Binding site ,Binding Sites ,biology ,Chemistry ,Temperature ,Proteins ,General Medicine ,Small molecule ,Research Papers ,Receptors, Mineralocorticoid ,Receptors, Androgen ,Liposomes ,Mutation ,biology.protein ,Nucleic acid ,protein–ligand complexes ,Carrier Proteins ,Protein ligand - Abstract
Methods presented for growing protein–ligand complexes fall into the categories of co-expression of the protein with the ligands of interest, use of the ligands during protein purification, cocrystallization and soaking the ligands into existing crystals., Obtaining diffraction-quality crystals has long been a bottleneck in solving the three-dimensional structures of proteins. Often proteins may be stabilized when they are complexed with a substrate, nucleic acid, cofactor or small molecule. These ligands, on the other hand, have the potential to induce significant conformational changes to the protein and ab initio screening may be required to find a new crystal form. This paper presents an overview of strategies in the following areas for obtaining crystals of protein–ligand complexes: (i) co-expression of the protein with the ligands of interest, (ii) use of the ligands during protein purification, (iii) cocrystallization and (iv) soaks.
- Published
- 2006