The crystallization of T. thermophilus tRNA^Asp complexed with its cognate aspartyl-tRNA synthetase is described. The Matthews coefficient has been determined and compared with those obtained for other aminoacylation systems.

The crystal structure of UK114 has been determined, revealing a trimeric arrangement. It was confirmed by ultracentrifugation studies that UK114 is also a trimer in solution.

Wild-type carbonic anhydrase II and mutant ElO6Q were found to bind acetate differently. In the mutant acetate is coordinated to the zinc ion but not in the wild-type enzyme.

Counter-diffusion crystallization using a new capillary crystallization format (CrystalHarp) is described. It allows low-temperature in situ diffraction data collection and is applicable for the novel high-pressure vitrification method, which allows data collection without the addition of cryoprotectant.