Conveners
Methods in Biocrystallography
- Jan Wollenhaupt (Helmholtz-Zentrum Berlin)
Our new environmental enclosure for fixed-target, serial crystallography enables full control of both the temperature and humidity. This enclosure provides access to time-resolved, X-ray diffraction experiments in a wide temperature range from below 10 °C to above 80 °C. We demonstrate changes in the electron density of a hyperthermophile enzyme as a function of increasing temperature and time.
Recently, it became possible to use CdTe Eiger detectors in macromolecular crystallography, enabling the use of high energy X-rays. Experiments at Diamond's beamline I24 could show that the theoretically predicted benefits of increased diffraction efficiency and photoelectron escape can indeed be exploited in the data collection of macromolecular crystals and data from huge protein complexes...
Here we present a novel conveyor belt-based sample delivery system for serial synchrotron crystallography (SSX). It is optimized for fast installation at beamlines, ease of use, low sample consumption and precise adjustment of several sample delivery parameters like ligand concentration, pH, sample temperature and delay time. Through combination of these parameters, CFEL TapeDrive 2.0 enables...
R-values represent the discrepancy between our macromolecular models and the measured X-ray data; they typically are around 20%, clearly showing that something is amiss; our current models of macromolecular crystal structures seem to be lacking. A better understanding of the shortcomings in our current models (and methods) could be an important factor to solving the most difficult structures...
Here, we describe the application of Spatially Resolved Anomalous Dispersion (SpReAD) refinement as a method to determine the oxidation state of protein-bound, small metal co-factors through x-ray crystallography, and show the influence of total absorbed dose on these experiments.
