Protein crystallization by surface entropy reduction: optimization of the SER strategy

A systematic study of the effect of substituting five different residues for large, solvent-exposed and flexible amino acids has been conducted using traditional and alternate reservoir screens. The results suggest a strategy that may enhance the success rates of preparation of X-ray quality crystals of proteins that are otherwise recalcitrant to crystallization in their wild-type form.

Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state

A 2.1 Å resolution crystal structure of the B. subtilis organic hydroperoxide-resistance protein B reveals details of the stereochemistry of the disulfide bonds in the transient oxidized form of the enzyme.