Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15 Å

The highest resolution structure of bacterial type II NADH:quinone oxidoreductase was determined at 2.15 Å resolution. This structure was used for in silico quinone substrate-docking studies to investigate the binding poses of menadione and ubiquinone molecules.

Crystal structure of the starch-binding domain of glucoamylase from Aspergillus niger

The crystal structure of the starch-binding domain of glucoamylase shows that the conformation of the region surrounding the disulfide bond is highly flexible.

Large-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP

The expression, large-scale crystallization and neutron diffraction analysis of the human HSP70 ATPase domain are reported.

Identification, biochemical characterization and crystallization of the central region of human ATG16L1

Structural information on the 607-amino-acid human ATG16L1 protein is restricted to the N-terminal ATG5-binding domain and the recently reported structure of the C-terminal WD40 domain, whereas structural information for the central region of ATG16L1 remains elusive. In this work, the identification, purification, biochemical characterization and crystallization of a stable ATG16L1 subfragment comprising residues 72–307, comprising the so far structurally uncharacterized central region of ATG16L1, are presented.

Crystallization and X-ray analysis of 23 nm virus-like particles from Norovirus Chiba strain

Virus-like particles (VLPs) from Norovirus Chiba strain were crystallized and data were collected to 3.2 Å resolution. X-ray analysis revealed that although 38 nm VLPs with T = 3 symmetry had been prepared for crystallization, the crystal contained 23 nm VLPs with T = 1 icosahedral symmetry.

Crystallization via tubing microfluidics permits both in situ and ex situ X-ray diffraction

Crystallization conditions for a pharmaceutical protein were optimized using a microfluidic platform and X-ray data were collected both in situ and ex situ.

Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis

The thermostabilities, hydrolytic properties and crystal structures of the OXA-48-like class D β-lactamases OXA-163, OXA-181 and OXA-245 have been investigated.