Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties

The three-dimensional structure of a human light-chain dimer (Sea) is reported to 1.94 Å resolution. This structure is likely to facilitate our understanding of why some seemingly harmless light chains display a propensity to aggregate as pathological amyloid fibrils.

Crystallization of the FAD-independent acetolactate synthase of Klebsiella pneumoniae

The crystallization and preliminary X-ray diffraction analysis of K. pneumoniae acetolactate synthase is reported. This enzyme is involved in the formation of 2-acetolactate which is the precursor of the branched-chain amino acids valine and leucine.