Protein structure is only as good as the data

Careful selection of the best diffraction geometry matched to the sample, with use of high resolution two-dimensional detectors and a mask integration procedure will allow the collection of statistically accurate data for many proteins and crystals with a sample size of at least 1 mm3. Accurate data and improved refinement techniques will allow the determination of all atoms including hydrogens, hydrogen-deuterium exchange, water of hydration, and solvent water densities. The developments in the above described neutron techniques have been gradually used in the analysis of myoglobins, gramicidin, trypsin, and crambin. 16 references, 11 figures, 2 tables