Proteins often form microcrystalline precipitates with an average size of crystallites (~ 0.1 - 1 μm) which in many cases are ideal for X-ray powder diffraction (XRPD). To date, a series of experiments and data analyses have been carried out, which demonstrate the validity of XRPD to study microcrystalline protein samples.

This method is powerful for high-throughput polymorph identification and crystal screening and also suitable for structure solution. In this webinar, we demonstrate the complementarity of laboratory and synchrotron XRPD as an analysis tool in protein crystallography. Parametric measurements (variation of relative humidity or pH) will be presented on pharmaceutical proteins and their complexes with organic ligands.
A question and answer session will conclude the presentation.
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