The crystal structure of bovine seminal ribonuclease, a homodimeric enzyme closely related to pancreatic ribonuclease, has been refined at a nominal resolution of 1.9/k employing data collected on an electronic area detector. The final model consists of two chains containing 1990 non-H atoms, seven sulfate anions and 113 water molecules per asymmetric unit. The unit-cell parameters are a = 36.5 (1), b = 66.7 (1) and c = 107.5(2)~,, space group P22~2~. The R factor is 0.177 for 16 492 reflections in the resolution range 6.0-1.9 A and the deviations from ideal values of bond lengths and bond angles are 0.020 A and 3.7", respectively. The molecule is formed by two pancreatic like chains, which have their N-terminal segments interchanged so that each active site is formed by residues from both subunits. The two chains are related by a non-crystallographic twofold symmetry and are covalently linked by two consecutive disulfide bridges, which form an unusual sixteen-membered ring across the dimer interface. The deviations from the molecular symmetry, the hydration shell and the sulfate-binding sites are also discussed in relation to the known structure of the pancreatic enzyme.

Crystals of the binary complex of alcohol dehydrogenase from Sulfolobus solfataricus with NADH were shown to be twinned and not suitable for automated data collection. Several crystallization trials, performed with the aim of eliminating twinning, are described. Interestingly, crystals grown from agarose gel have been demonstrated to have a unique reciprocal lattice. These crystals are monoclinic, space group C2, with cell dimensions a = 134.47 (9), b=85.26(5), c=71.76(8) A, /3=97.53(4) °, and showed significant diffraction beyond'3.0 A resolution.

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