A neutron diffractometer for biological macromolecules using neutron imaging plates

Abstract

Neutron imaging plates (NIPs), developed recently, have a good spatial resolution and availability of a large sensitive area. The NIPs having such characteristics may be particularly useful for neutron-diffraction measurements of biological macromolecules. We have constructed a neutron diffractometer dedicated to crystallography of biological macromolecules using the NIP, in the guide hall of the reactor JRR-3M at Japan Atomic Energy Research Institute. Neutrons are monochromatized with an elastically-bent-silicon monochromator ( λ = 0.22 nm). The diffraction patterns are detected with the NIP of 400 × 520 mm 2 at a distance of 150–300 mm from a sample crystal. A sequence of the measurements (exposure, reading the NIP, erasure of the pattern, and starting the next exposure) is done automatically. We measured the diffraction patterns from hen egg-white lysozyme crystals, and obtained the patterns which can be processed to derive integrated intensity of each diffraction spot.