Ultrahigh-resolution structure of high-potential iron–sulfur protein from Thermochromatium tepidum

The crystal structure of the high-potential iron–sulfur protein from T. tepidum was refined using low-temperature diffraction data to 0.80 Å resolution collected using synchrotron radiation. The electron transfer is discussed based on the hydrophobic interaction and molecular packing.

Crystallization and preliminary X-ray characterization of archaeal group II chaperonin α-­subunit from Thermococcus strain KS-1

The mutant α-subunit of group II chaperonin from Thermococcus strain KS-1 was crystallized. Diffraction data were collected to 2.4 Å with a synchrotron-radiation source.