Innovation versus practice in biological crystallization

Improving biological crystallization by innovation and publication.

Crystal structure of the catalytic subunit of bovine pyruvate de­hydrogenase phosphatase

The crystal structure of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase provides new insights into the mechanism of the regulation of the activity of the pyruvate dehydrogenase complex.

Tartryl-CoA inhibits succinyl-CoA synthetase

Human GTP-specific succinyl-CoA synthetase was produced, purified and crystallized from a solution containing tartrate and CoA. The crystal structure shows tartryl-CoA bound to the enzyme at 1.52 Å resolution.

Structural characterization of borneol de­hydrogenase from Pseudomonas sp. TCU-HL1

The structure of a Pseudomonas borneol dehydrogenase was determined at 1.84 Å resolution. Major differences from its homologues in the C-terminal helices and the associated loops may suggest determinants for substrate recognition.

A proposed carbon-utilization and virulence protein A, CuvA (Rv1422), from Mycobacterium tuberculosis H37Rv: crystallization, X-ray diffraction analysis and ligand binding

This study presents the crystallization, X-ray diffraction analysis and ligand binding of CuvA (Rv1422) from M. tuberculosis H37Rv and reports that MtCuvA can bind to the cell-wall precursor components uridine diphosphate (UDP)-glucose and UDP-N-acetylglucosamine.

Proline/alanine-rich sequence (PAS) polypeptides as an alternative to PEG precipitants for protein crystallization

The suitability of a PAS polypeptide as a precipitant to grow protein crystals with high X-ray diffraction quality has been demonstrated, adding this novel class of biosynthetic polymers to the toolset for protein crystallography as an alternative to polyethylene glycol.