Neutron photographic measurements of protein single-crystal reflections

Photographic neutron intensity measurements on a 2 mm³ single-crystal of triclinic lysozyme are compared with conventional neutron diffractometer data. The reflections were recorded with the oscillation technique. The structure factors were derived from the optical densities scanned by an automatic microdensitometer and processed by computer programs. A statistical analysis shows that the photographic data are of about the same accuracy as recently collected diffractometer data. For the same flux and crystal volume the data collection time is reduced by up to two orders of magnitude.