Expression, purification, crystallization and preliminary crystal structure analysis of the Deinococcus radiodurans organic hydroperoxide-resistance protein.
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 A resolution, have unit-cell parameters a = 45.7, b = 59.6, c = 49.7 A, beta = 90.43 degrees and belong to space group P2(1). The calculated Matthews coefficient of 2.1 A(3) 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.
Meunier-Jamin
Cécile
C
Macromolecular Crystallography Group, ESRF, BP 220, F-38043 Grenoble CEDEX, France.
Kapp
Ulrike
U
Leonard
Gordon
G
McSweeney
Seán
S
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003001:Cloning, Molecular / Q000379:methods; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D034301:Deinococcus / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
D001426:Bacterial Proteins; D011994:Recombinant Proteins