So how do you know you have a macromolecular complex?
Open Access
- 13 December 2006
- journal article
- review article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 63 (1) , 17-25
- https://doi.org/10.1107/s0907444906047044
Abstract
Protein in crystal form is at an extremely high concentration and yet retains the complex secondary structure that defines an active protein. The protein crystal itself is made up of a repeating lattice of protein-protein and protein-solvent interactions. The problem that confronts any crystallographer is to identify those interactions that represent physiological interactions and those that do not. This review explores the tools that are available to provide such information using the original crystal liquor as a sample. The review is aimed at postgraduate and postdoctoral researchers who may well be coming up against this problem for the first time. Techniques are discussed that will provide information on the stoichiometry of complexes as well as low-resolution information on complex structure. Together, these data will help to identify the physiological complex.Keywords
This publication has 32 references indexed in Scilit:
- A Dissection of Specific and Non-specific Protein–Protein InterfacesJournal of Molecular Biology, 2004
- The TB structural genomics consortium: a resource for Mycobacterium tuberculosis biologyTuberculosis, 2003
- Pathogenic α1-Antitrypsin Polymers Are Formed by Reactive Loop-β-Sheet A LinkageJournal of Biological Chemistry, 2000
- Quantitative characterization of reversible macromolecular associations via sedimentation equilibrium: an introductionExperimental & Molecular Medicine, 2000
- A Kinetic Mechanism for the Polymerization of α1-AntitrypsinPublished by Elsevier ,1999
- A soft, mean-field potential derived from crystal contacts for predicting protein-protein interactionsJournal of Molecular Biology, 1998
- New revolutions in the evolution of analytical ultracentrifugationCurrent Opinion in Structural Biology, 1996
- Dynamic light scattering studies of the aggregation of lysozyme under crystallization conditionsFEBS Letters, 1991
- Diagnostic of precipitant for biomacromolecule crystallization by quasi-elastic light-scatteringJournal of Molecular Biology, 1990
- Surface, subunit interfaces and interior of oligomeric proteinsJournal of Molecular Biology, 1988