|Protein Science Facility
At Protein Science Facility SWEDSTRUCT enables academic users to access high throughput protein production services and protein production expertise for a subsidized user fee composed of consumables, instruments, and university OH.
Protein Science Facility is also supported by ScilifeLab and Karolinska Institutet and offers in addition to protein production services access to infrastructure and user training in protein crystallography and protein characterisation.
Please see psf.ki.se for further information.
|Macromolecular Crystallography at MAX IV Laboratory
The MAX IV Laboratory, the successor of the MAX-lab national laboratory,
includes both the operation of the present MAX I, II and III facilities (MAX-lab) as well as the construction of the new MAX IV facility in Lund, Sweden.
The new facility will consist of a linac and two storage rings with 1.5 GeV and 3 GeV electron energy. The design of the 3 GeV storage ring uses a multibend achromats approach and it will be the first synchrotron using this new type of lattice.
The 3 GeV ring will have exceptionally low emittance which will lead to an unprecedented brilliance for a synchrotron radiation source.
BioMAX will be one of the seven initial beamlines at the new facility. It will be a high-throughput macromolecular crystallography (MX) beamline. It will offer high brilliance, tunable (0.5–2.5 Å wavelength), monochromatic X-rays with state-of-the-art performance in terms of low beam-divergence (0.1 mrad), high X-ray flux (~1013 photons/s) and variable beam size (10–100 μm), allowing work with both small crystals and large biomolecular complexes with concomitantly large unit cells. BioMAX is designed to be flexible and serve a broad range of needs for the life science community.
At the current MAX II storage ring we operate two beamlines for macromolecular crystallography, I911-2 and -3. The I911-3 beamline is energy tunable in the range between 6.2 – 16.5 keV (0.75 – 2.0 Å). The experimental setup includes a MD2 microdiffractometer with a MK3 mini-kappa, on-axis sample viewing, three-click centring and an Xflash silicon drift diode fluorescence detector. Diffraction data are collected using a Marmosaic 225 detector. The fluorescence detector can be used both for fluorescence scans (scanning the incoming X-ray beam energy over the absorption edge of a particular element) and measuring fluorescence spectra to, for example, quickly identify elements in the crystal. The beamline has a CATS automatic sample changer with a capacity of 90 samples using standard EMBL/ESRF pucks. The CATS sample changer can also be used for screening crystallisation plates for diffracting crystals. An EMBL Grenoble-type humidity control device (HC1) is available on request for optimising the diffraction properties of crystals or test samples at room temperature.
I911-2 is a fixed wavelength beamline (1.04 Å) equipped with a MarDTB goniostat and a Mar165 CCD detector. A suite of software packages is maintained for smooth data collection and analysis at the beamlines.
In addition, a small user laboratory including a crystallization facility is located within the current facility.
More general information on the MAX IV Laboratory can be found at www.maxlab.lu.se, for specific information for BioMAX see https://www.maxlab.lu.se/biomax and for the current MX beamlines https://www.maxlab.lu.se/node/34.
|Swedish NMR center
The Swedish NMR Centre at the University of Gothenburg comprises 7 NMR spectrometers in the range from 500 MHz to 900 MHz, with a focus on high-resolution NMR on biological macromolecules. The 900 MHz and the two 800 MHz spectrometers were recently equipped with Bruker Avance III HD consoles and triple resonance cryo-probes. The 900 MHz and one 800 MHz instrument are equipped with 5mm TCI-probes whereas the second 800 MHz spectrometers has a 5mm TXO-probe comprising cold 13C, 1H,15N and 2H coils and pre-amps. Furthermore, the 800 MHz spectrometers are equipped with automated sample changers. The three 600 MHz spectrometers are, in turn, dedicated to various research areas such as structural biology (Agilent HCN cold probe), solid-state spectroscopy (Agilent 2-channel XH-probe, 25 kHz MAS) and diffusion NMR (Bruker DRX with 5mm (1H,2H,13C, 19F) and 10mm (1H,19F) diffusion probes with a maximal gradient strength of 12 T/m).
The sample preparation laboratory offers access to standard equipment for protein handling, protein lyophilization and a Gilson Pipetting Robot for 96-well based NMR spectroscopy.
The staff at the Swedish NMR Centre provide assistance in cell-free protein expression for NMR purposes and targeted acquisition and automated sequential assignment of protein NMR spectra.
More general information on the Swedish NMR Centre can be found at www.nmr.gu.se.