01/10/03 - 14.2 Goes Robotic
01/10/03 - New Beamlines at the SRS
01/10/03 - Upgrades to the SRS
01/10/03 - DARTS Protein Crystallography Service
- How it works
11/09/03 - New Vision for NorthWest Science and Business
24/07/03 - Speak Out! and Listen - Speaker of the Year Award
14/07/03 - DARTS Cracks the 'Holy Grail'
of Nanoparticle Characterisation
22/05/03 - DARTS 2nd Technology Workshop
Protein Crystallography (PX) station 14.2 at the SRS has been providing high flux X-rays for single wavelength as well as Se-met MAD experiments since 1999. Life has just been made even better for 14.2 DARTS customers with the installation of an ACTOR system for automatic mounting and centring of protein crystals. The new system was commissioned during August 2003 by a team led by Steven Buffey, and the first external users were in early September 2003.
The system comprises a new camera, robot arm and storage dewar (combination of Rigaku/MSC and DL/Huber instrumentation), as well as new control software (PXGEN++). Currently only Hampton pins of length 18 mm can be mounted using the robot. For full specifications see:
http://www.msc.com/protein/documentation/ACTOR_pin.pdf
However, it is envisaged that the system will be further developed to allow automatic mounting of Oxford Cryosystems pins.
Crystals mounted in Hampton pins can be loaded into a magazine, which holds up to twelve samples. The storage dewar on the station can hold up to five magazines. Therefore a customer now has the ability to mount, screen and, if appropriate, collect data sets from up to sixty samples without any manual intervention in the data collection. Alternatively, DARTS customers may send their samples in magazines to Daresbury for data collection by in-house staff.
To view a short video of the robot in action, click here.
01/10/03 New Beamlines at the SRS
Beamline 11.1 is a new synchrotron infrared microspectroscopy facility that has recently been completed at Daresbury, and is now being commissioned ready for access by users. The beamline focuses the infrared synchrotron light down to a 10 micron spot which allows high spatial resolution chemical analysis of a wide range of materials from biological tissues to polymers, and from single crystals to archaeological remains. It is anticipated that the beamline will be further enhanced in the near future by the addition of an array detector infrared imaging system.
Beamline 12.1 provides unique structural information in solution from macromolecules such as proteins and carbohydrates. It has been operational for about a year, and is the world's leading synchrotron Circular Dichroism (CD) facility. The intensity and spectral range available from the synchrotron for CD allows greater accuracy of structure determination than is possible with conventional "bench top" CD instruments, and also allows millisecond time resolved measurements to be made of protein folding and molecular conformational dynamics.
It has been a long-standing goal of materials scientists and engineers to evaluate the intermediate stages of a manufacturing process accurately and on the same realistic time as the industrial plant, the ultimate aim being to directly correlate the microscopic structure of the material with its macroscopic physical properties. In order to achieve this goal high intensity X-rays are required coupled with detectors capable of high-count rate and excellent time resolution. A new station MPW6.2 has been specifically designed and constructed for this purpose and the combination of a 10-pole wiggler magnet, the Daresbury designed saggital focusing crystals and the X-ray mirrors provide a 1000-fold improvement in the X-ray flux to the experimental area. Detectors utilising RAPID readout electronics have been built with good spatial resolution in order to obtain quantitatively significant data.
The main techniques available on the station are very fast X-ray powder diffraction, wide angle X-ray scattering, small angle X-ray scattering and X-ray absorption spectroscopy. This station is dedicated to the study of materials processes and kinetic systems (e.g. crystallisation and/or nucleation) using any of the above techniques.
As many of you know, the SRS has been in shutdown for significant periods over the last 18 months. During this time there has been major investment in the development of the facilities available to the user community as well engineering works to improve the operational reliability of the facility.
The projects that have been completed are:
1) Completion of the storage ring modification for the North West Structural Genomics beamline MAD MPW10.
2) Completion of the EPSRC grant-funded new infra red microscope on beamline 11.
3) Completion of the BBSRC grant-funded circular dichroism station, CD12.
4) Completion of the EPSRC grant-funded MPW6.2 for materials processing.
5) Replacement of the mirror assembly on infra red line 13.3.
6) Replacement of the dipole 9 vacuum vessel.
7) Replacement of the insertion device vacuum vessel in straight 5 to allow the future installation of a new undulator.
8) A major upgrade of the liquid helium production plant for the two superconducting wigglers (9 and 16). This upgrade is essential to make up the efficiency deficit on the SC wigglers compared to storage ring operation and will secure reliable operations until 2008.
9) An internal modification to the 6 tesla superconducting wiggler to improve its heat loss characteristics and hence its requirement from the helium production plant.
10) Installation of new passive loads on the storage ring RF to improve the
ease of maintenance.
It was necessary to vent 1.5 sectors of the SRS to complete this work, which led to significant disruption to normal user operations. However, all of these projects have now been completed successfully and users are experiencing the benefits. The unusually hot summer affected the lifetime recovery but now we are back to normal Warrington weather, the SRS is operating at 2 fills a day with efficiencies during MB operation consistently in excess of 95%.
01/10/03 DARTS Protein Crystallisation Service - How it Works
Pharmaceutical companies are in the business of producing drugs designed to interact with specific protein targets. The drug/target interaction is first tested in order to elicit an effect, either boosting the protein's biological activity or reducing it. To fine tune the interaction, further detailed information is usually required, which often means structure determination of the protein coupled to its target molecule. DARTS is well disposed to offer a complete protein crystallisation service to satisfy your needs.
As the customer, you may want to provide DARTS with a 'ready to use' concentrated sample i.e. stable at 5 - 10 mgml-1, monodisperse and with known characteristic profiles. DARTS can pre-check these characteristics after shipping either by SDS-PAGE or UV-VIS in addition to DLS measurements to assess monodispersity. DLS can also be applied to determine the most suitable temperature and/or pH for producing crystals. If stability is an issue during transportation, DARTS can provide a range of final purification steps and concentration of dilute protein samples.
DARTS uses commercial crystallisation screens to probe 100-200 different conditions at two different temperatures. The initial screen requires 500 µl of concentrated protein. The screen is then refined until diffraction quality crystals are obtained. Most common crystallisation problems arise due to poorly ordered protein crystals such as those with glycosylation sites containing flexible sugar molecules or membrane proteins with a high solvent content and containing detergent molecules. DARTS can also try crystallisation conditions that have already been reported in the literature for similar target proteins.
DARTS staff have been successful in crystallising a number of globular
and membrane proteins e.g. light-harvesting complexes, plant lectins and bacterial
phosphatases. Some of these crystals diffracted to atomic resolution (better
than 1.2 Å). In addition, staff are technically adept in data acquisition,
structure solution and refinement. This powerhouse of expertise can be made
available for the most pressing needs of today's pharmaceutical industries.
We are confident that DARTS can provide a service to suit your needs.
11/09/03 New Vision for Northwest Science and Business
A new vision for the development of a groundbreaking campus concept at Daresbury Laboratory was signed on the 10th of September by CCLRC and the NWDA. The new campus will provide a crucial link between business, the world-leading Daresbury Laboratory and its university research teams.
Further information may be obtained from the NWDA Press Release. The photograph below shows 'work in progress'
24/07/03 Speak Out! and Listen - Speaker of the Year Award
Congratulations to Chris Pickles, the DARTS Marketing Manager who has won the Chemical Industry Association's Experienced Speaker of the Year Award 2003.
Further information about this award can be found at the Chemical Industry Association (CIA) website
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14/07/03 - DARTS cracks the 'Holy Grail' of Nanoparticle Size Measurement
Small angle X-ray scattering (SAXS) at the Daresbury Laboratory can now be used to measure the size distribution of 'true' nanoparticles in the 1-100 nm range, using specific experimental conditions and advanced data treatment developed on site. The technique has the flexibility to cope with samples either in liquid suspension or dry powder form, and most importantly can determine particle size distribution - a key requirement of particle size analysis on this scale.
Avecia research manager John Conti-Ramsden applauded the development of this exciting new technology and commented: "nanoparticles are becoming increasingly important in the development of advanced materials for a variety of industrial applications, and the ability to accurately monitor and control particle size and distribution at these levels is critical."
Powders made up of nanoparticles have application in areas such as controlled-release drug delivery, biotechnology, IT, telecommunications and printing of 'devices' and are used by manufacturers of cosmetics, pigments, clays, prints and catalysts.
In the electronics industry, nanoparticle powders are being used to 'build up' rather than 'etch out' nanostructures. Until now, the major limiting factor has been the inability to accurately determine nanoparticle size distributions. Traditionally particle size analysis has been performed using light scattering, where the interference patterns from lasers are used to measure nanoparticle size. Because many nanopowders are smaller than the wavelength of visible light, these methods have a lower limit of 100 nm. The DARTS breakthrough now extends measurement capability to orders of magnitude below this limit.
22/05/03 The Second DARTS International Workshop
The Second DARTS Technology Workshop was held at Daresbury on the 21st of May. There were speakers representing all of the main services offered by DARTS - click here for a copy of the programme.
The photograph above shows participating speakers (left to right):
Chris Pickles, DARTS Marketing Manager
Chris Hall, University of Edinburgh
Ian Tickle, Astex Technology Ltd
Elizabeth MacLean, DARTS General Manager
Rob Slinger, Canadian Light Source Inc
Lee Fielding, Organon Laboratories Ltd
Jeff Cutler, Canadian Light Source Inc
Bob Cernik, Daresbury Laboratory