Statistical surveys of protein structures reveal that the backbone conformation in terms of (φ, ψ) is the most important factor in τ-angle modulation.

Large diffracting crystals of alcohol dehydrogenase from Sulfolobus solfataricus were grown in microgravity. Improvement of size and diffraction resolution limit was also observed.

Statistical surveys of protein structures combined with quantum-mechanical calculations reveal a systematic dependence of bond distances on conformation. Interestingly, the variability of backbone C—O and C—N distances is not directly related to peptide-bond planarity.

The crystal structure of the P235GK mutant of the arginine-binding protein from Thermotoga maritima in its monomeric state provides clues to the structural determinants of the domain swapping observed in the wild-type protein.