| Abstract: | Synchrotron radiation (SR) techniques are continuously pushing the frontiers of wavelength range usage, smaller crystal sample size, larger protein molecular weight and complexity, as well as better diffraction resolution. The new research specialism of probing functional states directly in crystals, via time-resolved Laue and freeze trapping structural studies, has been developed, with a range of examples, based on research stretching over some 20 years. Overall, SR X-ray biological crystallography is complemented by neutron protein crystallographic studies aimed at cases where much more complete hydrogen details are needed involving synergistic developments between SR and neutron Laue methods. A big new potential exists in harnessing genome databases for targeting of new proteins for structural study. Structural examples in this tutorial review illustrate new chemistry learnt from biological macromolecules. |
