- Protein Crystallography
- IµS-Cu MX for PX
- METALJET for PX
Single crystals of macromolecules and proteins are usually very small and show only poor diffraction thus making the determination of such crystal structures a challenging task. In general, the interaction of electromagnetic radiation with matter increases with the wavelength approximately by the power of three. The use of Cu-Kα radiation, therefore, results in a more efficient diffraction compared to e.g. Mo-Kα or Ag-Kα and usually leads to a reasonable atomic and spatial resolution of the diffraction pattern. This is indispensable in particular for crystal structures with long cell axes.
Incoatec microfocus source IµS in combination with a mardtb
Diffraction pattern of the carbonic anhydrase crystal recorded with the IμS
X8 PROSPECTOR with a Cu-IμS MX microfocus X-ray source equipped with a MX optics and APEXII CCD detector
Diffraction pattern of the endothiapepsin crystal
Protein Crystallography with IµS-Cu MX
The Cu-IµS MX is the brightest microfocus sealed tube for X-ray diffraction currently available. It delivers a two-dimensional focused beam with an unprecedented flux density of > 2.0 x 1010 phts/s/mm2 Cu-Kα radiation giving a performance beyond traditional 5 kW rotating anode systems with second generation multilayer mirrors, such as Montel 200 or Osmic Blue mirrors. The high intensity and the excellent beam stability guarantees high data quality for applications such as crystal screening and S-SAD phasing. The beam cross-section of the image focus is about 0.11 mm (FWHM). The dedicated and patented mirror housing allows easy and reliable alignment. An optional variable aperture at the exit of the housing enables the reduction of the beam divergence in order to resolve long unit cell axes. The Cu-IµS MX is a reliable and easy-to-use X-ray source for compact, but powerful solutions in structural biology.
Now our latest IµS DIAMOND source exploits the extreme conductivity of diamond to achieve intensities of up to 6 x 1010 phts/s/mm2, exceed the intensity of most rotating anodes sources.
The METALJET X-ray source in a D8 VENTURE
Diffraction pattern of a small protein crystal, measured with a Bruker AXS D8 VENTURE equipped with the Excillum METALJET X-ray source
Protein Crystallography with METALJET
The METALJET X-ray source was developed in collaboration with Excillum and Bruker AXS to become the brightest and most intensive microfocus X-ray source available today outside of synchrotron beamlines. This revolutionary new liquid metal source technology is designed to meet the ever-increasing demands of modern structural biology, and particularly of protein crystallography and of small angle X-ray scattering. Together with its low cost of ownership and its ease-of-use, the METALJET is the X-ray source of choice for high-end research laboratories.
The METALJET X-ray source for protein crystallography uses focusing HELIOS MX Ga optics that contain synchrotron-class quality multilayer mirrors delivering the smallest and most intensive X-ray beam of any home-lab X-ray source with up to 3 times the intensity of modern microfocus rotating anodes. The metal target is a molten Ga rich alloy, giving a wavelength of 1.34 Å which is very close to the wavelength of Cu anodes (1.54 Å). Therefore, the METALJET is well suited for most challenging applications, such as fast screening of large and weakly diffracting protein complexes or structure determination by S-SAD phasing.