MX Beamline Instumentation
Macromolecular crystallography has evolved over the past year towards fully automated systems. However, for the most challenging projects, optimal conditions still need fine tuning and dedicated instruments. As Beamline Scientist on the microfocus MX beamline I24, Armin assisted in the design, construction and commissioning towards first user experiments of this very successful beamline. He then continued as Principal Beamline Scientist for the long-wavelength MX beamline I23. He designed this beamline as a unique instrument dedicated towards solving the phase problem from native proteins and nucleic acids without the need of labelling or prior knowledge of similar structures. The beamline is radically different to existing beamlines and required dedicated solutions to overcome the challenges arising from the long wavelengths needed for these experiments.
Native phasing from native proteins and nucleic acids
The long-wavelength MX beamline is optimised for a wavelength range not accessible at any other synchrotron instrument. Its aim is to solve difficult structure via experimental phasing techniques such as SAD and MAD. The main focus of Armin's research will be to systematically investigate effects of X-ray absorption on the data quality and its potential correction to exploit the longest wavelengths available at the beamline and determine and provide the optimal receipes for measuring and analysing data from this unique instrument. The increased anomalous signal at the long-wavelengths will open native phasing methods to projects of increased complexity.
Detectors for in-vacuum long-wavelength diffraction experiments
During his postdoc at the Swiss Light Source, Armin has worked closely with the detector group and solved the very first protein structure from the Pilatus 1M detector. For the I23 project a vacuum compatible detector with high sensitivity in the long-wavelength range was needed and in collaboration with Dectris the Pilatus technology was successfully tested at the Diamond beamlines I18 and B16. The I23 Pilatus 12M detector is currently the largest detector for protein crystallography at synchrotrons operating at a vacuum level of < 10E-7 mbar down to wavelengths > 5 A.
Sample handling and mounting
For both microfocus and long-wavelength experiments small signals need to be measured accurately. A main focus of Armin's work is to find suitable materials for sample mounts and reduce the access solvent around crystals to reduce the scattering brackground from the additional material which only contributes to noise and not to signal. He successfully used laser tweezers for mounting microcrystals to fibre coated sample mounts and helped to establish sample mounting procedures on Si chips for serial crystallography experiments at both synchrotrons and XFEL sources.