Methods for separating nucleation and growth in protein crystallisation.
The availability of high-quality crystals is crucial to the structure determination of proteins by X-ray diffraction. With the advent of structural genomics the pressure to produce crystals is greater than ever before. Finding favourable conditions for crystallisation is usually achieved by screening of the protein solution with numerous crystallising agents. Optimisation of the crystallisation conditions involves the manipulation of the crystallisation phase diagram with the aim of leading crystal growth in the direction that will produce the desired results. This article highlights recent advances in experimental methods for improving crystal size and quality by separating the nucleation and growth phases of crystallisation using the vapour diffusion and microbatch techniques.
Chayen
Naomi E
NE
Biological Structure and Function Section, Division of Biomedical Sciences, Sir Alexander Fleming Building, Imperial College London, Exhibition Road, London SW7 2AZ, UK. n.chayen@imperial.ac.uk
D020650:Combinatorial Chemistry Techniques / Q000295:instrumentation* / Q000379:methods; D003460:Crystallization / Q000295:instrumentation / Q000379:methods*; D008832:Microchemistry / Q000295:instrumentation* / Q000379:methods; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000032:analysis / Q000737:chemistry; D036103:Nanotechnology / Q000295:instrumentation / Q000379:methods; D044367:Phase Transition; D011506:Proteins / Q000032:analysis* / Q000737:chemistry*; D012371:Robotics / Q000295:instrumentation / Q000379:methods*; D013048:Specimen Handling / Q000295:instrumentation / Q000379:methods*
D046912:Multiprotein Complexes; D011506:Proteins