Analysis of the different redox states of the catalytic cysteines in four crystallographic structures of thioredoxin 1 from the Pacific whiteleg shrimp L. vannamei highlights their reactivity and corroborates the existence of a structural dimer mediated by an interface of 12 residues which includes a disulfide bridge between the Cys73 residues of each monomer.
The cocrystal structure of the PTB domain of integrin cytoplasmic domain-associated protein-1 (ICAP1) in complex with a 29-residue fragment of Krev/Rap1 interaction trapped-1 (KRIT1) has been determined.
The 3-hydroxyacyl-CoA dehydrogenase from Ceanorhabditis elegans was overexpressed, purified and crystallized in two different space groups (P1 and P212121). The molecular dimers found in one asymmetric unit from both space groups are identical but each packs in a distinct manner.
Aldehyde dehydrogenase (ALDH) catalyses the oxidation of aldehydes using NAD(P)+ as a cofactor. The aldh gene from B. cereus was cloned; the protein was expressed, purified and crystallized, and a preliminary X-ray crystallography analysis was performed.
The L. donovani coronin CRN12 coiled-coil domain (5.8 kDa) was cloned, overexpressed and purified to homogeneity. Crystals of recombinant L. donovani coronin CRN12 coiled-coil domain were grown by vapour diffusion using a hanging-drop setup.
The Escherichia coli cyclic AMP receptor protein (CRP) crystals were obtained and diffracted at a 2.9 Å resolution, which belonged to the space group P3121, with unit-cell parameters a = b = 76.03, c = 144.00 Å. The asymmetric unit was found to contain one protein molecule and a half 38 bp full-length double-stranded DNA fragment with a Matthews coefficient of 2.62 Å3 Da−1 and a solvent content of 53.14%.
EaLsc, a levansucrase from E. amylovora, has been cloned, expressed, purified and crystallized. X-ray crystallographic analysis and data collection to 2.77 Å resolution have been carried out. The structure was solved by molecular replacement and refinement is in progress.
The pyridoxal biosynthesis lyase (PdxS) from Mycobacterium tuberculosis was crystallized and diffracted to a resolution of 1.8 Å. The crystals were found to belong to space group I222 or I212121, with unit-cell parameters a = 110.75, b = 126.08, c = 180.82 Å, α = β = γ = 90°.