Fast, flexible single crystal X-ray diffractometer with the latest generation sources and HPC X-ray detectors, perfect for any crystallography lab.
With your success utmost in our minds, we have developed the XtaLAB Synergy-S X-ray diffractometer for single crystal X-ray diffraction. Using a combination of leading edge components and user-inspired software tied together through a highly parallelized architecture, the XtaLAB Synergy-S produces fast, precise data in an intelligent fashion. The system is based around the PhotonJet-S series of microfocus X-ray sources that incorporate continuously variable divergence slits. These third generation sources have been designed to maximize X-ray photons at the sample by using a combination of new optics, new, longer life, tubes and an improved alignment system. PhotonJet-S are available in Cu, Mo or Ag wavelengths in either a single or dual source configuration. 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 your diffraction experiment. The system is also equipped with your choice of HPC X-ray detector, including the HyPix-6000HE, PILATUS3 R 200K, PILATUS3 R 300K or EIGER 1M.
- Extremely high performance due to bright source, noise-free X-ray detector and fast goniometer speeds
- Continuously variable divergence slit option lets you resolve reflections from long unit cells.
- Minimal downtime with longer X-ray tube lifetime — supported by online diagnostics and troubleshooting
- Compact design to fit in your laboratory
- Cryostream 800 (Oxford Cryosystems)
- Cobra (Oxford Cryosystems)
- Product name: XtaLAB Synergy-S
- Technique: Single crystal X-ray diffraction
- Benefit: 3D structural analysis of molecules
- Technology: Single crystal X-ray diffractometer
- Core attributes: Single or dual X-ray source diffractometer with hybrid pixel array detector and kappa goniometer
- Core options: Cryostream or Cobra cooler (Oxford Cryosystems) and XtalCheck-S
- Computer: External PC, MS Windows, CrysAlis Pro
- Core dimensions: 130,0 (W) x 187,5 (H) x 85,0 (D) cm
- Mass: 550 kg (core unit)
- Power requirements: 1Ø, 90-130V 15A or 180-260V 4A
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.
Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization
Konstantin S. Usachev, Bulat F. Fatkhullin, Evelina A. Klochkova, et al.
Journal of Structural Biology
Staphylococcus aureus hibernation promoting factor (SaHPF) is responsible for the formation of 100S ribosome dimers, which in turn help this pathogen to reduce energy spent under unfavorable conditions. Ribosome dimer formation strongly depends on the dimerization of the C-terminal domain of SaHPF (CTDSaHPF). In this study, we solved the crystal structure of CTDSaHPF at 1.6 Å resolution and obtained a precise arrangement of the dimer interface. Residues Phe160, Val162, Thr171, Ile173, Tyr175, Ile185 and Thr187 in the dimer interface of SaHPF protein were mutated and the effects were analyzed for the formation of 100S disomes of ribosomes isolated from S. aureus. It was shown that substitution of any of single residues Phe160, Val162, Ile173, Tyr175 and Ile185 in the SaHPF homodimer interface abolished the ribosome dimerization in vitro.