So how do you know you have a macromolecular complex?
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.
Dafforn
Timothy R
TR
Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, England. t.r.dafforn@bham.ac.uk
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D019281:Dimerization; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D006860:Hydrogen Bonding; D046911:Macromolecular Substances / Q000737:chemistry*; D008968:Molecular Conformation; D011506:Proteins / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry; D013696:Temperature; D014461:Ultracentrifugation; D014965:X-Rays
D046911:Macromolecular Substances; D011506:Proteins; D012997:Solvents