The structure of Rv0802c was determined in an unliganded form to 2.0 Å resolution utilizing single-wavelength anomalous dispersion from a samarium soak that resulted in a single bound Sm3+:citrate2 complex.
This paper describes how four general optimization techniques, growth-rate modulation, fine screening, seeding and additive screening, have been adapted for automation in a medium-throughput crystallization service facility.
In order to determine the protonation states of the residues within the active site of an HIV-1 protease–inhibitor complex, a crystal of HIV-1 protease complexed with inhibitor (KNI-272) was grown to a size of 1.4 mm3 for neutron diffraction study. The crystal diffracted to 2.3 Å resolution with sufficient quality for further structure determination.
Exo-α-1,5-L-arabinofuranosidase from S. avermitilis NBRC14893 was crystallized by the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.2 Å and belonged to space group P212121.
Xoo2316 from X. oryzae pv. oryzae, a predicted 6-phosphogluconolactonase, the second enzyme of the pentose phosphate pathway, has been cloned, purified and crystallized. A native data set was collected to 2.4 Å resolution and a MAD data set was collected to 2.5 Å resolution.
Crystals of the nucleocapsid protein of human respiratory syncytial virus have been obtained in two forms, the better of which diffracted to 3.6 Å resolution and contained ten subunits in the asymmetric unit.
Peptide deformylase (PDF) catalyzes the removal of the N-formyl group from the N-terminus of nascent polypeptides. This process is essential for the survival of bacteria. As it is an antibacterial drug target, PDF from X. oryzae pv. oryzae was cloned, purified and crystallized for preliminary X-ray studies.
BTL2, a thermostable enantioselective biocatalyst of interest for industrial applications, has been crystallized using the sitting-drop vapour-diffusion method. Preliminary X-ray data to 2.2 Å resolution allowed the determination of its unit-cell parameters and space group and initiation of its structure determination.
MTH909, the M. thermautotrophicus orthologue of S. cerevisiae TAN1, has been overexpressed, purified and crystallized. X-ray data were collected to 2.85 Å resolution from a crystal belonging to space group P6122 (or P6522).
The putative enolase MJ0232 from M. jannaschii was purified and crystallized. A native data set was collected to 1.85 Å resolution. Preliminary crystallographic analysis and a dynamic light-scattering experiment suggested biological relevance of the octameric state of MJ0232 in solution.