Overexpression, crystallization and preliminary X-ray crystallographic analysis of the phosphotriesterase from Mycobacterium tuberculosis

Crystals of the phosphotriesterase from M. tuberculosis were obtained and diffraction data were collected and processed to 2.27 Å resolution. An analytical ultracentrifugation experiment suggested that mPHP exists as dimers in solution.

Complex assembly, crystallization and preliminary X-ray crystallographic analysis of the chicken MHC class I molecule BF2*1501

X-ray diffraction data were collected to 2.6 Å resolution from a crystal of the chicken MHC class I molecule BF2*1501. The crystal belonged to space group P3₁21, with unit-cell parameters a = 125.1, b = 125.1, c = 80.9 Å, and contained two molecules in the asymmetric unit. The Matthews coefficient and solvent content were calculated to be 2.08 ų Da⁻¹ and 40.78%, respectively.

Crystallization and preliminary X-ray crystallographic analysis of the human CKIP-1 pleckstrin homology domain

Crystals of an S84D/S86D/S88D triple mutant of the casein kinase 2 interacting protein-1 (CKIP-1) pleckstrin homology domain were obtained and diffraction data were collected and processed to 1.7 Å resolution.

Preliminary X-ray diffraction analysis of octaprenyl pyrophosphate synthase from Escherichia coli

Here, Escherichia coli octaprenyl pyrophosphate synthase was expressed, purified and crystallized. The crystals were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.2 Å resolution.

Crystallization and preliminary structural analysis of dibenzothiophene monooxygenase (DszC) from Rhodococcus erythropolis

The structure of DszC from R. erythropolis DS-3 was solved using the single-wavelength anomalous dispersion method.

Crystallization and preliminary crystallographic studies of GRASP65 GRASP domain from Rattus norvegicus

The GRASP65 GRASP domain from R. norvegicus has been expressed, purified and crystallized. The crystals belonged to space group P2₁2₁2, with unit-cell parameters a = 44.99, b = 104.29, c = 37.93 Å, and diffracted to 2.0 Å resolution.

Preliminary crystallographic analysis of RraB from Escherichia coli

The crystallization and preliminary X-ray diffraction analysis of the ribonuclease regulator RraB from E. coli are reported.