The 1.6 Å structure of a semisynthetic RNase from 43% aqueous ethanol closely resembles the 1.8 Å structure obtained from crystals grown in concentrated salt solution, although a major difference is the positioning of active-site residue His119.

A preliminary X-ray diffraction study is reported of the homo-tetramers of hemoglobins II and III of the symbiont-harboring clam Lucina pectinata.

Dihydroorotase from the extreme hyperthermophile A. aeolicus was cloned and expressed at high levels in E. coli. Crystals of the purified wild type and selelnomethionine-substituted enzyme, space group C2, diffracted to a resolution of 1.7 Å.

One complex of thrombin-hirudin₅₁₋₆₅ in the asymmetric unit was located by molecular replacement; the second complex was found by visual inspection of electron-density maps. Molecular replacement could locate the second complex only after the contribution of the first molecule had been subtracted from the structure factors by density modification.