A conserved core in the SufE sulfur-acceptor protein mediates interdomain interactions in variety of redox protein complexes

Purification and crystallographic studies of a D-alanyl-D-alanine carboxypeptidase from B. stearothermophilus

Three-dimensional structure of actinoxanthin at 2.5 Å resolution

Crystallization and preliminary X-ray study of OXA-1, a class D β-lactamase

The OXA-1 oxacillinase from E. coli has been crystallized from PEG at pH 7.5 in P1. Crystals diffract to 1.5 Å resolution and contain two monomers related by a pseudo twofold screw axis.

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A conserved core in the SufE sulfur-acceptor protein mediates interdomain interactions in variety of redox protein complexes

Purification and crystallographic studies of a D-alanyl-D-alanine carboxypeptidase from B. stearothermophilus

Three-dimensional structure of actinoxanthin at 2.5 Å resolution

Crystallization and preliminary X-ray study of OXA-1, a class D β-lactamase

search results

results of search on CRYSTALLOGRAPHY JOURNALS ONLINE

A conserved core in the SufE sulfur-acceptor protein mediates interdomain interactions in variety of redox protein complexes

Purification and crystallographic studies of a D-alanyl-D-alanine carboxypeptidase from B. stearothermophilus

Three-dimensional structure of actinoxanthin at 2.5 Å resolution

Crystallization and preliminary X-ray study of OXA-­1, a class D β-lactamase

Crystallization and preliminary X-ray study of OXA-1, a class D β-lactamase