| Literature DB >> 24385107 |
Parveen Pahuja1, Alagiri Srinivasan, Munish Puri.
Abstract
X-ray crystallography for the determination of three-dimensional structures of protein macromolecules represents an important tool in function assignment of uncharacterized proteins. However, crystallisation is often difficult to achieve. A protein sample fully characterized in terms of dispersity may increase the likelihood of successful crystallisation by improving the predictability of the crystallisation process. To maximize the probability of crystallisation of a novel mouse macrophage protein (rMMP), target molecule was characterized and refined to improve monodispersity. Addition of MgCl2 at low concentrations resolves the rMMP into a monodisperse solution, and finally successful crystallization of rMMP was achieved. The effect of MgCl2 was studied using gel filtration chromatography and dynamic light scattering.Entities:
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Year: 2014 PMID： 24385107 DOI： 10.1007/s11010-013-1934-x
Source DB: PubMed Journal: Mol Cell Biochem ISSN： 0300-8177 Impact factor: 3.396