Giant Synchrotron to be Constructed in UK

juntunen writes "According to the BBC, construction will start this week on Diamond: a £500 million synchrotron in Oxfordshire at the Rutherford Appleton Laboratory. These facilities are crucial to a deep understanding of structure in matter. With all the new emphasis on biotechnology, demand will certainly be high. Diamond has its own homepage, and the Accelerator Physics Group has publicly available tech notes."

Comments

Re:Couple of questions...

[Anonymous Coward]

One thing that synchrotrons are great at is producing high power x-rays, which have applications in both material science and high power microscopy. This x-ray production is actually almost a byproduct of the main application, which is usally smashing beams of subatomic particles together to better understand what they're made of.

Controversial Siting

[seanellis]

The new facility, Diamond, will be housed at Rutherford Appleton Laboratories near Oxford. There was a concerted effort to get the project sited at the existing synchrotron facility at Daresbury.

The reasons for siting at Daresbury seemed to be well thought out and sensible - see the campaign website for more information.

The government has decided to site it in the expensive South of England, putting the existing synchroton research team at Daresbury in jeopardy and virtually guaranteeing a dispersal of talent.

Re:Controversial Siting

[kgp]

Daresbury in addition to being the birthplace of Lewis Carrol (Charles Luttwidge Dodgson -- there's a neat stained glass window in the church where his father was vicar) was also the site of the first dedicated storage ring for generating synchrotron radiation (i.e. polarized light from IR to hard X-ray).

Originally the site was created to extend particle physics in the North of England (to include a collaboration of the "northern universities": Liverpool, Manchester, Leeds, Hull. A particle physics 5GeV electron synchrotron called NINA was built there in the early to mid 1970s and did some useful work.

It also attracted a new group of condensed matter physicists (surface scientists too) who used the synchrotron radiation emitted to do spectroscopy and diffraction of various sorts (photelectron spectrosocopy in the extreme UV and soft X-ray where the SR sources are particularly bright compared to other sources). They set up the SRF to try out these ideas.

The NSF (Nuclear Structure Facility -- for doing energetic heavy ion collisions -- nothing to do with nuclear weapons!) was built there in the late 1970s. That's the tower you can see in the site pictures. Unfortunatly SERC killed nuclear structure work in the UK in 1990. They pulled funding for the NSF and told people to look for beamtime at other sites outside the country. In fact the Recoil Seperator ended up at Oak Ridge, TN (so they didn't keep that expertise in the country).

http://www.srs.ac.uk/srs/

NINA was decomissioned in the late 1970s and it was decided to build the Synchrotron Radition Source (SRS) using part of the old NINA site (and the NINA linac, I think) to provide a dedicated SR source in the UK for chemists, biologists, martials scientists and physicists.

All though this time a theory group was based there and a large regional computing facility (that used to have a Cray 1 in the good old days from 1979 to 1983) that was a major node on JANET (the academic network in the UK).

The SRS was comissioned in 1982. This is where the 20 years mentioned in the article comes in -- opened in 1982 and closed in 2003(ish). I not sure if they'll keep the SRS open although the parameters for the SRS and DIAMOND are rather different. DIAMOND is good for high brightness X-ray studies but not so good for soft X-ray or XUV uses.

I worked there as a (suface science) grad student (from Liverpool University) and got my PhD working on the TGM and GIM and SEXAFS stations on beamline 6 and later did some work on Beanline 1 when I worked at the Surface Science Center at Liverpool University.

The site had a lot of experitise for machine physics (the epople who understand how to keep the electrons going around the ring), beamline and monochromator design. I suspect some of these will move down south and another nothern resource will be lost.

I'm sure the RAL people are happy (the decision as made almost 2 years ago) but they don't have a site who boundary is formed by the Bridgewater Canal. Perhaps it's heading the same way as that old tech.

Kevin Purcell
Beamline 6 (and 1)
University of Liverpool.

SSC

[QEDog]

The huge accelerator was called Superconducting Super Collider. Its purpose was different. It would reach higher energies.

This new acceleratos will only reach about 3.5GeV. Much less than FermiLab's TeV accelerator, so its mail goal is not to discover new sub-atomic particles (as those energies have been studied before) but to have biological applications.

Re:oh that's great...

[jma34]

I'm pretty sure that this accelerator is used more as a light source and not for finding particles. I just looked briefly at the documents but they all seemed to be dealing with the light beam rather than the actual particle beam. I don't think that there are going to be any great particle discoveries from this accelerator, but there will certainly be some very, verry cool pictures take. I was working at the Cornell Synchrotron and they had some awesome pics of the cold virus that they had taken using the x-rays of their beam.

Re:Couple of questions...

[Bowling Moses]

To answer the third question first: organism have a truly massive number of proteins encoded in their genome, (almost) all of which have a specific and well-defined 3-dimensional structure. Currently the structures for several thousand proteins have been determined, and the structures are deposited at the Protein Data Bank (PDB). Most of these are solved using xray crystallography, which is part of what I'm studying. We've learned that if you are carefull, you can coax purified protein to crystallize rather than just fall out of solution in an uniteresting and useless glop. Hampton Research is one company specializing in supplies relating to the crystallization of proteins, and has some pictures of protein crystals on their site. It had been known for a long time that if you put a nice ordered object (like a crystal) into an xray beam, you would get a diffraction pattern from it. The diffraction pattern can tell you some information about the internal makeup of the crystal, such as how big the repeating unit of the crystal is (crystals are made up of a large number of small units that are stacked next to each other in a lattice). Eventually it was found that you could rotate the crystal in the beam and collect many diffraction patterns from different angles and with a large amount of effort calculate the structure of the molecules in the crystal. In the bad old days in the 60's this meant that you hired a couple of math majors to be human calculators and after five years you would have your protein structure. With computers you can go from data collection to solved structure in only a few months.

I don't quite get the "20 years" thing either. The Advanced Light Source (ALS) at Berkeley was built in 1942, or at least the original building was. It has naturally gone through a number of upgrades, the last being a totally new synchrotron built in 1987-93?. I don't know about wear and tear on the facility but we've found that as far as macromolecular crystallography (usually meaning proteins) goes, xray intensity is no longer an issue. A complete data set collected at the Advanced Photon Source at Argonne Nat'l Labs took me less than an hour. That's just 1 second exposures to xrays as opposed to up to an hour or more on our lab's xray source. The big change occuring at synchrotrons for macromolecular crystallography is automation--it takes more time for a newbie to get trained and get set up for their first collection than to actually collect their data, but robotics for this kind of thing are relatively new--also data processing and structure determination is still very time consuming. Structural genomics (basically have structures of all the proteins in an organism determined) is also taking off and automation is a Very Big Thing for them as they screen 100,000's of protein crystals--Syrrx is probably the most advanced at this so far. Of course the problem with structural genomics is that you generate 100's of structures that lay around uniterpreted--a process that still requires a human touch. Anyway, hope that's some help.