|Title||Can Protein Conformers Be Fractionated by Crystallization?|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Authors||Xu, AS, Li, FL, Robinson, H, Yeung, ES|
|Type of Article||Article|
|Keywords||alkaline-phosphatase, beta-galactosidase, complex, dynamics, electrophoretically-mediated microanalysis, energy, enzyme, individual molecules, kinetics, molecules, single-molecule|
, different crystals, even when grown from the same drop of mother liquor, showed markedly different activities. Activities of individual molecules from a crystal were found to be essentially identical, whereas molecules obtained directly from solution showed a 4-fold variation in activity. Furthermore, after storage at 37 degrees C, the distribution of single-molecule LDH activities from solutions of individual crystals broadened and approached that of LDH obtained from the original solution. X-ray crystallography also showed distinct conformations for single microcrystals and confirms that crystallization properly selects even small conformational variants of proteins and that the slow equilibration to multiple stable conformations in solution is responsible for the observed single molecule heterogeneity.
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