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A high-speed data-collection system for large-unit-cell crystals is presented, using the Fuji Imaging Plate as an X-ray detector and a rotating-anode generator as the X-ray source. It is an automatic data-acquisition system that requires almost no manual intervention. The quality of data collected on the system is discussed. Merging R values ranged from 0.04 to 0.05. Compared with a four-circle diffractometer, data reproducibility was better, isomorphous/anomalous Patterson maps were almost identical in quality and data from a small-molecule crystal, cytidine, were of almost the same quality. Protein structures were refinable using the data measured on the system, the final crystallographic R value of the 2.2 Å 3-isopropylmalatedehydrogenase structure being 0.185 and that of the 1.88 Å Flammulina veltipes agglutinin structure being 0.199.
Sato et al. (1992) studied this question.