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Crystallization and preliminary X-ray diffraction analysis of the full-length Mg2+ transporter MgtE.

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.

SUBMITTER: Hattori M

PROVIDER: S-EPMC2335169 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the full-length Mg2+ transporter MgtE.

Hattori Motoyuki M Tanaka Yoshiki Y Fukai Shuya S Ishitani Ryuichiro R Nureki Osamu O

Acta crystallographica. Section F, Structural biology and crystallization communications 20070721 Pt 8

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 SeM ...[more]

PMID: 17671367

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