Crystallographic analysis and phasing of iron-assimilating protein 1 (FEA1) from Chlamydomonas reinhardtii

In Chlamydomonas reinhardtii, iron levels are strictly controlled by iron-assimilating protein 1 (FEA1). Recombinant FEA1 protein was successfully purified and crystallized by hanging-drop vapor diffusion. The phase problem was solved by the native sulfur SAD method using long-wavelength X-rays (2.7 Å). Laser-cutting technology was used to increase the signal-to-noise ratio and derive an initial structure.

A new crystal form of GABARAPL2

A new untwinned crystal form of the autophagy protein GABARAPL2 is described. The LC3-interacting region (LIR) docking site is blocked by a crystal contact with the C-terminal residue, Phe117. This residue is removed during the processing of GABARAPL2 by Atg4 family proteases. This suggests that the removal of Phe117 is required to co-crystallize LIR peptides with GABARAPL2 in order to establish the interactions between these important autophagy mediators.

Crystal structure of enoyl-CoA hydratase from Thermus thermophilus HB8

Enoyl-CoA hydratase (ECH) catalyzes the second step of the β-oxidation pathway. Here, the crystal structure of ECH from T. thermophilus HB8 is reported at 2.85 Å resolution.

Simplified heavy-atom derivatization of protein structures via co-crystallization with the MAD tetragon tetra­bromoterephthalic acid

Tetrabromoterephthalic acid (B4C) provides sufficient anomalous signal to solve the crystal structure of hen egg-white lysozyme using MAD phasing. The use of B4C as an experimental phasing compound offers several advantages over existing compounds, including its compatibility with common crystallization reagents and its amenability to co-crystallization.