On the routine use of soft X-rays in macromolecular crystallography.
A diffraction data set has been collected from a blood coagulation factor XIII-Ca(2+) complex crystal at the X-ray diffraction beamline of the ELETTRA synchrotron (Trieste, Italy) at a wavelength of 2.6 A. The data collection could be carried out using the beamline as is, without making any time-consuming changes to the apparatus. Various data-processing schemes have been employed and it has been observed that local or detector scaling procedures are essential for producing the 'best' anomalous differences.
Weiss
M S
MS
Institute of Molecular Biotechnology, Department of Structural Biology and Crystallography, PO Box 100813, D-07708 Jena, Germany. msweiss@imb-jena.de
Sicker
T
T
Djinovic-Carugo
K
K
Hilgenfeld
R
R
D018360:Crystallography, X-Ray / Q000295:instrumentation* / Q000379:methods; D005583:Fourier Analysis; D010088:Oxidoreductases / Q000737:chemistry*; D010231:Paracoccus denitrificans / Q000201:enzymology; D011487:Protein Conformation; D014965:X-Rays
D010088:Oxidoreductases; C022763:nitrous oxide reductase