Synergy S
XtaLAB Synergy-S is the dual-microfocus sealed tube X-ray source diffractometer with hybrid pixel array (photon counting) detector and kappa goniometer. The system is equipped with an Oxford Cryostream 800 cryo-head for sample temperature control from 80 – 400K. Room temperature, in-plate X-ray data collection is also possible using the XtalCheck-S adapter.
This machine can be used to collect X-ray diffraction data for chemical crystallography and protein structure determination.
Chemical Crystallography
The XtaLAB Synergy S single crystal X-ray diffractometer comes with kappa goniometer that incorporates fast motor speeds and a unique telescopic two-theta arm to provide total flexibility for the diffraction experiment. The system is also equipped with a HyPix-6000HE detector and intense dual sources including Mo-Kα and Cu-Kα X-radiation, which covers all the usual requirements for chemical crystallography. Sample can be run at the temperatures ranging from 80K up to 373K. Data collection times can range from a matter of minutes to 2-3 hours depending on the sample. Powder samples can also be run either in capillary tubes or as slurries in oil for phase identification of bulk samples. See this poster of experimental electron densities from accurate X-ray Diffraction data.
Protein Crystallography
Cryo-crystallography
The detector has a relatively small active area (77.5 mm x 80.3mm) because it is a direct, digital photon counting detector. With this detector, the complete X-ray diffraction data sets with high quality can be collected from cryo-cooled protein crystals. This is possible by the inclusion of a fast kappa geometry goniometer that allows data collection scan speeds of up to 10°/sec. The continuously variable divergence slits can be used to resolve unit cell dimensions up to xx Å - xxx Å. See this poster of data collection from a single cryo-cooled crystal of Hen Egg White Lysozyme (HEWL) to demonstrate Sulphur SAD phasing.
In-plate X-ray diffraction
The XtalCheck-S system includes software that facilitates both visual and diffraction imaging of crystallization experiments. With the XtalCheck-S system, many crystallization experiments can be surveyed by eliminating the need to harvest and cryo-cool samples. Moreover, serial crystallography experiments can be performed, by collecting data from multiple crystals, to achieve complete data sets that can be used for structure solution.
