M. Schiltz et al., PROTEIN CRYSTALLOGRAPHY AT ULTRA-SHORT WAVELENGTHS - FEASIBILITY STUDY OF ANOMALOUS-DISPERSION EXPERIMENTS AT THE XENON K-EDGE, Journal of synchrotron radiation, 4, 1997, pp. 287-297
A protein crystallography experiment at the xenon K-edge (lambda = 0.3
58 Angstrom) has been successfully carried out at the materials scienc
e beamline (BL2/ID11) of the ESRF. The samples used in this methodolog
ical study were crystals of porcine pancreatic elastase, a 26 kDa prot
ein of known structure. The diffraction data are of excellent quality.
The combination of isomorphous replacement and anomalous dispersion o
f a single xenon heavy-atom derivative allowed accurate phase determin
ation and the computation of a high-quality electron density map of th
e protein molecule. This is the first fully documented report on a com
plete protein crystallography experiment, from data collection up to p
hase determination and calculation of an electron density map, carried
out with data obtained at ultra-short wavelengths. Experimental consi
derations as well as possible advantages and drawbacks of protein crys
tallography at very short and ultra-short wavelengths are discussed.