ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Can the propensity of protein crystallization be increased by using systematic screening with metals?

Hegde, Raghurama P and Pavithra, Gowribidanur C and Dey, Debayan and Almo, Steven C and Ramakumar, S and Ramagopal, Udupi A (2017) Can the propensity of protein crystallization be increased by using systematic screening with metals? In: PROTEIN SCIENCE, 26 (9). pp. 1704-1713.

[img] PDF
Pro_Sci_26-9_1704_2017.pdf - Published Version
Restricted to Registered users only

Download (655kB) | Request a copy

Abstract

Protein crystallization is one of the major bottlenecks in protein structure elucidation with new strategies being constantly developed to improve the chances of crystallization. Generally, well-ordered epitopes possessing complementary surface and capable of producing stable inter-protein interactions generate a regular three-dimensional arrangement of protein molecules which eventually results in a crystal lattice. Metals, when used for crystallization, with their various coordination numbers and geometries, can generate such epitopes mediating protein oligomerization and/or establish crystal contacts. Some examples of metal-mediated oligomerization and crystallization together with our experience on metal-mediated crystallization of a putative rRNA methyltransferase from Sinorhizobium meliloti are presented. Analysis of crystal structures from protein data bank (PDB) using a non-redundant data set with a 90% identity cutoff, reveals that around 67% of proteins contain at least one metal ion, with similar to 14% containing combination of metal ions. Interestingly, metal containing conditions in most commercially available and popular crystallization kits generally contain only a single metal ion, with combinations of metals only in a very few conditions. Based on the results presented in this review, it appears that the crystallization screens need expansion with systematic screening of metal ions that could be crucial for stabilizing the protein structure or for establishing crystal contact and thereby aiding protein crystallization.

Item Type: Editorials/Short Communications
Publication: PROTEIN SCIENCE
Additional Information: Copy right for this article belongs to the WILEY, 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
Department/Centre: Division of Physical & Mathematical Sciences > Physics
Date Deposited: 30 Sep 2017 09:20
Last Modified: 03 Oct 2018 14:33
URI: http://eprints.iisc.ac.in/id/eprint/57934

Actions (login required)

View Item View Item