XtaLAB mini II
A benchtop single crystal X-ray diffractometer with the latest technology HPC X-ray detector, ideal for self-service crystallography.
Single crystal X-ray diffraction on your benchtop
The Rigaku XtaLAB mini II, benchtop X-ray crystallography system, is a compact single crystal X-ray diffractometer designed to produce publication-quality 3D structures. The perfect addition to any synthetic chemistry laboratory, the XtaLAB mini II will enhance research productivity by offering affordable structure analysis capability without the necessity of relying on a departmental facility. With the XtaLAB mini II, you no longer have to wait in line to determine your structures. Instead your research group can rapidly analyze new compounds as they are synthesized in the lab.
Teach single crystal X-ray diffraction through hands-on experience
In many universities, the departmental single crystal X-ray diffractometer is considered off limits to students because of fear that the instrument might be damaged by inexperienced users. The XtaLAB mini II provides the opportunity for students to learn single crystal X-ray analysis by actually using a fully functional diffractometer. This is not a black box instrument. Rather, the important step of mounting a crystal on the goniometer and physically centering the crystal in the position of the X-ray beam, ensures that students learn the importance of mounting techniques and crystal selection. The simple design of the XtaLAB mini II X-ray diffractometer minimizes the danger of students damaging the system.
Reduced size does not mean reduced data quality
The Rigaku XtaLAB mini II is a research grade chemical crystallography instrument that sits on the benchtop. No data quality compromises, no extended collection times. Results delivered are unambiguous. X-ray source tube lifetime is extended by running at 600 W. To compensate for running at a lower power, a SHINE optic (special curved monochromator) is utilized to produce usable X-ray flux comparable to a standard X-ray diffractometer.
Dedicated to producing publication quality single crystal X-ray structures
The chief design requirement when creating the XtaLAB mini II was that the structures produced would be publishable in the most demanding scientific journals. The HPC X-ray detector is positioned so that the maximum 2θ value is well outside of the Acta Cryst. requirements. The software provides all the tools you need to generate publication quality data that can be used to determine 3D structures from a variety of structure analysis packages.
- Affordable design with low operating costs
- Requires minimal training and support
- Automatic structure solution software
- Provides definitive structural information
- Ideal supplement for a NMR spectrometer
- Perfect self-serve departmental lab instrument
- Ideal teaching instrument
- Publication quality results
- Air-cooled HPC detector
- No special infrastructure required (110 VAC)
- Optional cryosystem available
- Cryostream 800 (Oxford Cryosystems)
- Smartstream (Oxford Cryosystems)
- Product name: XtaLAB mini II
- Technique: Single crystal X-ray diffraction
- Benefit: Benchtop structural characterization
- Technology: Benchtop X-ray diffractometer with advanced detector
- Core attributes: 600 W Mo X-ray tube, hybrid photon counting detector
- Core options: Cryostream or Smartstream (Oxford Cryosystems)
- Computer: External PC, MS Windows, CrysAlis Pro software
- Core dimensions: 56,0 (W) x 67,4 (H) x 39,5 (D) cm
- Mass: 100 kg (core unit)
- Power requirements: 1Ø, 100-240 V 50/60 Hz
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.