D.M. Blow

TL;DR: In this article, Rossmann and Blow describe how they have detected the existence of partial, approximate symmetry from a knowledge of the intensities alone, and the effect of noncrystallographic symmetry, whether partial or total, results in decreasing the size of the structure to be determined, while the number of observable intensities remains the same.

TL;DR: Refined atomic co-ordinates for tosyl-α-chymotrypsin have been obtained by computational refinement of co-coordinates derived from a carefully built atomic model as mentioned in this paper.

TL;DR: A detailed analysis of the binding of N-formyl-l-tryptophan to the active site of α-chymotrypsin shows that the indolyl side chain lies in a hydrophobic pocket or slit, which accounts for the specificity of this enzyme for binding arginine or lysine side chains.

TL;DR: In this article, the positions and orientations of the inhibitor groups were determined from difference Fourier projections calculated using phase angles derived from a single isomorphous heavy-atom derivative.