In this paper, which is freely available to all readers, Frank Sargent and colleagues have isolated a stable and cofactor-free complex of the cytoplasmic chaperone protein TorD with the TorA (trimethylamine N-oxide reductase) apoenzyme, both with and without the twin-arginine signal peptide, and using a combined biophysical and biochemical approach show that a single TorD monomer binds directly to a single TorA apoprotein regardless of the presence of the signal peptide.

In this paper, Udo Oppermann, Wyatt Yue and colleagues have determined the crystal structures of all catalytic (MAT1A and MAT2A) and regulatory (MAT2B) subunits of the human MAT (methionine adenosyltransferase) family and present results which provide the first atomic view of the eukaryotic MAT2B architecture, allow a comparison of the MAT1A/MAT2A active site with structural homologues to be made, and establish a molecular basis for MAT disease mutations.

In this paper, Peter Rotwein and colleagues have identified a haemojuvelin/RGMc (repulsive guidance molecule c) molecular species containing four disulfide linkages: the first structural information obtained for any member of the RGM family.

In common with a number of other journals, from 1 December authors submitting a paper reporting the structure of a biological macromolecule to the Biochemical Journal must also provide the PDB Validation Report (after annotation by the wwPDB) for the information of the reviewers.