Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit

Authors: Hall, Pamela R.; Zheng, Run; Pusztai-Carey, Marianne; van den Akker, Focco; Carey, Paul R.; Yee, Vivien C.

Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 521-523(3)

Publisher: Blackwell Publishing

Key:

- Free Content

- New Content

- Subscribed Content

- Free Trial Content

Abstract:

The dimeric outer 5S subunit of transcarboxylase has been expressed in three different forms and crystallized: native 5S, 5S-His₆ and selenomethione-5S-His₆. All the crystals have an orthorhombic space group, but while native 5S forms primitive orthorhombic crystals, 5S-His₆ crystals are either C-centered or primitive and SeMet-5S-His₆ crystals are C-centered. Crystallization of native 5S requires the addition of lithium sulfate, whereas this salt prevented crystallization of 5S-His₆. All 5S crystals diffract to ∼2.0 Å resolution with synchrotron radiation. Efforts are under way to solve the structure of SeMet-5S-His₆ using MAD.

Keywords: transcarboxylase; Propionibacterium shermanii; lithium sulfate

Document Type: Research article

DOI: 10.1107/S0907444903028294

The full text electronic article is available for purchase. You will be able to download the full text electronic article after payment.

$50.16 plus tax Refund Policy