The first crystal structure of the RBM39-UHM–U2AF65-ULM complex has been determined at 2.2 Å resolution. Comparison to other UHM–ULM complexes reveals both common and unique interactions.

The method of X-ray footprinting mass spectrometry was used to investigate the effect of X-ray irradiation on various proteins in solution under both fully aerated and low dissolved oxygen conditions, and as a function of protein concentration.

Alkyl hydroperoxide reductase from Anabaena sp. PCC 7120 was expressed, purified and crystallized. Diffraction data to 2.5 Å resolution revealed that the crystals belonged to space group P2₁2₁2₁, with unit-cell parameters a = 80, b = 102, c = 109.6 Å.

This work describes the expression, purification, circular dichroism spectrum and crystallization of a central domain from human Splicing Factor 1. A native, 2.5 Å resolution data set is reported.

Crystals have been grown from a recombinant form of hORF6 that is a member of the novel antioxidant enzyme family. A native data set has been collected to 2.0 Å resolution.

The overproduction, purification and crystallization of the organic hydroperoxide-resistance protein from D. radiodurans are described. The crystals are monoclinic, space group P2₁, with unit-cell parameters a = 45.7, b = 59.6, c = 49.7 Å, β = 90.43°. Preliminary X-ray diffraction data have been collected.