XtaLAB Synergy Custom

Rigaku XtaLAB Synergy Custom

Single crystal X-ray diffractometer with custom enclosure and flexibility for easy integration of accessory components.


Rigaku realize that standard systems may not fit the needs for every lab, so we also offer XtaLAB Synergy Custom single crystal X-ray diffractometers for those labs who want to take advantage of dual ports or want to integrate special components, such as ACTOR sample changers. Additionally, for laboratories that want even greater flux we offer the FR-X based diffraction systems.

  • Customized systems for structural biology and chemical crystallography utilizing a high flux microfocus source
  • Your choice of VariMax confocal double-bounce optics for better spectral purity and beam size to match your sample types
  • Four-circle goniometer to provide completeness and redundancy for your data sets
  • HPC detector with single pixel point spread function and true shutterless data collection
  • Dual ports allow for various combinations of crystallography and SAXS ports
  • Options for in situ crystallography and automated mounting for cryo-protected samples

HPC detector

XtaLAB Synergy Custom systems are configured with a Hybrid Photon Counting (HPC) X-ray detector, such as the HyPix-6000HE, PILATUS or EIGER. HPC detectors are ideal for macromolecular crystallography experiments because they are photon counting detectors that directly detect X-ray photons without the need for the intermediate step of converting X-ray photons to light with a phosphor or scintillator. As a result, HPCs have high dynamic range, fast readout speed and extremely low noise. Additionally, HPC X-ray detectors have a top-hat point spread function of a single pixel. These combined features, along with shutterless data collection, mean that you can collect more accurate diffraction data, faster. As a result, the XtaLAB Synergy Custom systems offer outstanding performance for macromolecular single crystal X-ray diffraction experiments.

Dual Port Capability

XtaLAB Synergy Custom system includes a dual port, microfocus rotating anode X-ray generator. With XtaLAB Synergy Custom systems, you can configure to have dual single crystal ports or you can configure the second port with a small angle X-ray scattering system, such as the BioSAXS-2000. Additionally, the XtaLAB Synergy Custom comes in a custom designed enclosure with your choice of table size, to accommodate accessory equipment, such as an ACTOR system or microscope close to the goniometer. Thus, the versatility offered by the XtaLAB Synergy Custom system provides the most flexibility possible for your structural biology program.


  • Cryostream 800 (Oxford Cryosystems)
  • Cobra (Oxford Cryosystems)
  • ACTOR
  • ELement ANalyzer
  • XtalCheck
  • Product name: XtaLAB Synergy Custom
  • Technique: Single crystal X-ray diffraction
  • Benefit: 3D structural analysis of molecules
  • Technology: Customizable single crystal X-ray diffractometer
  • Core attributes: X-ray diffractometer with rotating anode X-ray source and HPC detector
  • Core options: Cryostream or Cobra cooler (Oxford Cryosystems), ACTOR, BioSAXS-2000, Dual Port
  • Computer: External PC, MS Windows, CrysAlis Pro
  • Core dimensions: Varies with configuration
  • Mass: Varies with configuration
  • Power requirements: Varies with configuration

Crystals are regular arrays of atoms, and X-rays can be considered waves of electromagnetic radiation. Atoms scatter X-ray waves, primarily through the atoms’ electrons. Just as an ocean wave striking a lighthouse produces secondary circular waves emanating from the lighthouse, so an X-ray striking an electron produces secondary spherical waves emanating from the electron. This phenomenon is known as elastic scattering, and the electron (or lighthouse) is known as the scatterer. A regular array of scatterers produces a regular array of spherical waves. Although these waves cancel one another out in most directions through destructive interference, they add constructively in a few specific directions, determined by Bragg’s law. X-ray diffraction results from an electromagnetic wave (the X-ray) impinging on a regular array of scatterers (the repeating arrangement of atoms within the crystal). X-rays are used to produce the diffraction pattern because their wavelength is typically the same order of magnitude (1–100 angstroms) as the spacing between planes in the crystal. In principle, any wave impinging on a regular array of scatterers produces diffraction, as predicted first by Francesco Maria Grimaldi in 1665. To produce significant diffraction, the spacing between the scatterers and the wavelength of the impinging wave should be similar in size. For illustration, the diffraction of sunlight through a bird’s feather was first reported by James Gregory in the later 17th century. The first artificial diffraction gratings for visible light were constructed by David Rittenhouse in 1787, and Joseph von Fraunhofer in 1821. However, visible light has too long a wavelength (typically, 5500 angstroms) to observe diffraction from crystals. Prior to the first X-ray diffraction experiments, the spacings between lattice planes in a crystal were not known with certainty.The idea that crystals could be used as a diffraction grating for X-rays arose in 1912 in a conversation between Paul Peter Ewald and Max von Laue in the English Garden in Munich. Ewald had proposed a resonator model of crystals for his thesis, but this model could not be validated using visible light, since the wavelength was much larger than the spacing between the resonators. Von Laue realized that electromagnetic radiation of a shorter wavelength was needed to observe such small spacings, and suggested that X-rays might have a wavelength comparable to the unit-cell spacing in crystals. Von Laue worked with two technicians, Walter Friedrich and his assistant Paul Knipping, to shine a beam of X-rays through a copper sulfate crystal and record its diffraction on a photographic plate. After being developed, the plate showed a large number of well-defined spots arranged in a pattern of intersecting circles around the spot produced by the central beam. Von Laue developed a law that connects the scattering angles and the size and orientation of the unit-cell spacings in the crystal, for which he was awarded the Nobel Prize in Physics in 1914.