Protein crystallization: from purified protein to diffraction-quality crystal.
Determining the structure of biological macromolecules by X-ray crystallography involves a series of steps: selection of the target molecule; cloning, expression, purification and crystallization; collection of diffraction data and determination of atomic positions. However, even when pure soluble protein is available, producing high-quality crystals remains a major bottleneck in structure determination. Here we present a guide for the non-expert to screen for appropriate crystallization conditions and optimize diffraction-quality crystal growth.
Chayen
Naomi E
NE
Department of Biomolecular Medicine, Division of Surgery, Oncology, Reproductive Biology and Anaesthetics, Faculty of Medicine, Imperial College London, Sir Alexander Fleming Building, London SW7 2AZ, UK. n.chayen@imperial.ac.uk
Saridakis
Emmanuel
E
D002627:Chemistry, Physical / Q000379:methods*; D003460:Crystallization / Q000379:methods*; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure*; D012031:Refractometry / Q000379:methods*
D046912:Multiprotein Complexes; D011506:Proteins