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 MgCl 2 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.
Original language | English |
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Pages (from-to) | 133-139 |
Number of pages | 7 |
Journal | MOLECULAR AND CELLULAR BIOCHEMISTRY |
Volume | 389 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - Apr 2014 |
Keywords
- Crystallisation
- Dispersity
- Dynamic light scattering
- Gel filtration chromatography