First protein structure solved using the JUNGFRAU detector!
JUNGFRAU is a charge-integrating, two-dimensional pixel detector developed at the Paul Scherrer Institut for use at free-electron lasers, in particular SwissFEL, and synchrotron light sources. On the 10th October, the first protein crystallography experiment using the JUNGFRAU detector, was performed at the beamline X06SA (PXI) of the Swiss Light Source by the members of the Protein Crystallography and Detectors groups at PSI.
Diffraction from single, native insulin crystal was recorded on two JUNGFRAU modules consisting of one million pixels in total. The data were of excellent quality, as judged by the overall crystallographic data statistics. It was possible to perform de novo structure determination from this data using single-wavelength anomalous diffraction phasing method. This result demonstrates that the quality of diffraction data recorded using the JUNGFRAU detector is sufficient for obtaining accurate measurements of Bragg peak intensities, which were necessary for successful structure solution.
Diffraction from single, native insulin crystal was recorded on two JUNGFRAU modules consisting of one million pixels in total. The data were of excellent quality, as judged by the overall crystallographic data statistics. It was possible to perform de novo structure determination from this data using single-wavelength anomalous diffraction phasing method. This result demonstrates that the quality of diffraction data recorded using the JUNGFRAU detector is sufficient for obtaining accurate measurements of Bragg peak intensities, which were necessary for successful structure solution.
Diffraction pattern from insulin crystal recorded using the JUNGFRAU detector (top). Electron density maps, after phasing with SHARP (left), after solvent flattening with DM (middle), final map after refinement (right).