Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit.
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Hall PR, Zheng R, Pusztai-Carey M, van den Akker F, Carey PR, Yee VC
Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit.
Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):521-3. Epub 2004 Feb 25.
- PubMed ID
- 14993680 [ View in PubMed]
- Abstract
The dimeric outer 5S subunit of transcarboxylase has been expressed in three different forms and crystallized: native 5S, 5S-His(6) and selenomethione-5S-His(6). All the crystals have an orthorhombic space group, but while native 5S forms primitive orthorhombic crystals, 5S-His(6) crystals are either C-centered or primitive and SeMet-5S-His(6) crystals are C-centered. Crystallization of native 5S requires the addition of lithium sulfate, whereas this salt prevented crystallization of 5S-His(6). All 5S crystals diffract to approximately 2.0 A resolution with synchrotron radiation. Efforts are under way to solve the structure of SeMet-5S-His(6) using MAD.