Structural analysis appts. for monocrystal - utilises processor control of crystal rotation for recording reflected ray indices and intensity

摘要

Detailed structural analysis of a fragile crystal such as protein is performed by measuring diffraction of X-rays to obtain reflections as the crystal is rotated. The reflections are detected for recording. A crystal (2) is subjected to bombardment of X-rays through a collimator (3). Two linear position detectors (4) are located on a turntable (5) moved by step motors (6, 7). A third step motor (8) rotates about a vertical axis (mu). Optical benches (9) permit movement of the detectors relative to the crystal. The crystal is rotated under processor control to accumulate detector data of reflected X rays on storage discs. The indices and intensities of the reflexions are calculated for each plane.