Structure of the imine reductase from Ajellomyces dermatitidis in three crystal forms

The structure of the imine reductase from A. dermatitidis is presented in three crystal forms, each of which provides information on conformational dynamics and cofactor and substrate binding within the enzyme.

Drastic alterations in the loop structure around colchicine upon complex formation with an engineered lipocalin indicate a conformational selection mechanism

Colchicalin is an engineered binding protein derived from the lipocalin scaffold, which provides a binding site comprised of four loops exhibiting structural plasticity. Structural analysis of this lipocalin in the absence and the presence of its ligand colchicine reveals drastic structural changes which indicate a conformational selection mechanism.

High-resolution crystal structure of the Mu8.1 conotoxin from Conus mucronatus

The crystal structure of the Mu8.1 conotoxin was determined in the high-symmetry space group I4₁22 at 1.67 Å resolution. This crystal structure reveals a surface-exposed Zn²⁺-binding site and establishes a hydrogen-bonding network around Lys55 buried at the dimer interface.