Expression, purification, crystallization and preliminary crystal structure analysis of the Deinococcus radiodurans organic hydroperoxide-resistance protein

Authors: Meunier-Jamin, Cécile; Kapp, Ulrike; Leonard, Gordon; McSweeney, Seán

Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 920-922(3)

Abstract:

The organic hydroperoxide-resistance protein (DR1857) from Deinococcus radiodurans has been expressed, purified and crystallized. The crystals are suitable for X-ray analysis, diffract to at least 2.3 Å resolution, have unit-cell parameters a = 45.7, b = 59.6, c = 49.7 Å, β = 90.43° and belong to space group P2₁. The calculated Matthews coefficient of 2.1 Å³ Da⁻¹ coupled with a calculated solvent content of approximately 42% is consistent with the presence of a homodimer in the asymmetric unit. Here, the methods used in the overexpression and purification of the protein are described and details of crystallization conditions and preliminary X-ray diffraction are provided.

Keywords: organic hydroperoxide-resistance protein; Deinococcus radiodurans; 2-Cys peroxidase

Document Type: Research article

DOI: 10.1107/S0907444904003993

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

$50.39 plus tax Refund Policy