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Updated: Jul 13, 2026
Assessing Two-dimensional Crystallization Trials of Small Membrane Proteins for Structural Biology Studies by Electron Crystallography
Published on: October 29, 2010
Crystallization and preliminary X-ray diffraction analysis of the full-length Mg2+ transporter MgtE
Motoyuki Hattori1, Yoshiki Tanaka, Shuya Fukai
1Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan.
Abstract:
The MgtE family of Mg(2+) transporters are ubiquitously conserved in all three domains. The genes encoding full-length MgtE from seven different species were cloned. Three of the seven MgtE transporters were overexpressed and purified for use in crystallization trials. Only Thermus thermophilus MgtE was successfully crystallized using the sitting-drop vapour-diffusion method. Selenomethionine-substituted (SeMet) crystals were obtained by cross-microseeding using the native microcrystals. The SeMet crystals diffracted X-rays to 3.5 A resolution using synchrotron radiation and belong to space group C222(1), with unit-cell parameters a = 118.3, b = 134.9, c = 366.2 A. Structure determination is in progress.
