Purification, crystallization and preliminary crystallographic analysis of human dihydrodipicolinate synthase-like protein (DHDPSL)

A human enzyme, DHDPSL, which is homologous to bacterial pyruvate-dependent aldolases but of unknown function, has been expressed, purified and crystallized with the use of in situ proteolysis. The crystals diffracted to 2.0 Å resolution and were suitable for structure determination.

Another case of fraud in structural biology

Editorial.

Purification, crystallization and preliminary crystallographic analysis of the adhesion domain of Epf from Streptococcus pyogenes

The putative adhesion domain of the multidomain protein Epf from S. pyogenes has been crystallized in space groups P2₁ and P2₁2₁2₁. The crystals diffracted to 2.0 and 1.6 Å resolution, respectively, at the Australian Synchrotron.

Use of a repetitive seeding protocol to obtain diffraction-quality crystals of a putative human D-xylulokinase

A putative human D-xylulokinase enzyme has been expressed, purified and crystallized using a repetitive seeding protocol. The trigonal crystals belonged to space group P3₁ or P3₂, with unit-cell parameters a = b = 101.87, c = 158.85 Å, and diffracted X-rays to at least 2.7 Å resolution.