History Structural Biology files The SRS for Structural Biology

Establishment of the SRS as the home for structural biologists


The efforts to make the SRS the home for structural molecular biology dates as far back as the establishment of the NINA SRF. To understand some complexity, it is worth mentioning that the UK’s Science Research Council (SRC) established NINA and subsequently the SRS at Daresbury. There were a number of other research councils at the time including the Medical Research Council and the Agricultural and Food Research Council, each jealously guarding their territories and budgets. Simply said, anyone outside the scope and remit of the SRC had to get their funding council to pay their way for the use of the NINA SRF but more so for the SRS owing to what was a significant investment by a single research council.

Max Perutz (MRC Cambridge), David Phillips (Oxford Molecular Biophysics) and Maurice Wilkins (King’s College) represented the interests of the MRC at meetings on 22nd January and 3rd August 1973. It was clear that at the time, the main beneficiary was expected to be fibre diffraction and as such Hugh Huxley was nominated to coordinate the activities at the NINA SRF. Huxley was able to obtain impressive static diffraction pictures from frog muscle (see below) in early 1974 and was able to progress towards initial time resolved muscle diffraction using this synchrotron source before the closure of NINA on 31st March 1977. In 1978 when Joan Bordas moved to EMBL Hamburg, where fibre diffraction and XAFS instruments had been located on the storage ring DORIS, Hugh Huxley joined in the effort. He only returned to the SRS in the mid 1980s. Joan returned to Daresbury as the head of MRC’s Structural Biology Laboratory in 1983. At his time MRC also decided to build a dedicated beamline 2.1 for biological solution scattering and fibre diffraction.

X-ray picture

John Helliwell, who was a DPhil student at Oxford with Dr Margaret Adams, attended the 10th IUCr Congress in Amsterdam in August 1975 where he heard Keith Hodgson (Stanford) talk about some early crystallographic experiments performed at the 3.7GeV SPEAR storage ring at Stanford (eventually reported in PNAS, 73, 128-132, 1976). When he asked his supervisory team to go to Stanford to gain experience, he was taken to David Phillips who told him about the existence of the Daresbury Synchrotron Radiation Facility. This turned out to be good fortune for the development of crystallographic activities (see article by John Helliwell). It also clearly showed how important the 1973 meeting was where David Phillips was present. John obtained his beamtime on the NINA SRF in December 1976 but the tests were unfortunately inconclusive, primarily due to insufficient intensity and the operating mode of NINA – one would have to wait until the storage ring came on line providing steady intensity. In the meantime, elsewhere in Europe, Roger Fourme put together a dedicated facility for protein crystallography on the positron storage ring DCI at LURE using an electronic detector (Nuclear Instruments & Methods, 152, 173-177 (1978)), which began to attract users, including some from the UK, as the news of possible gains of up to 20 over a 24 kW Elliott GX6 rotating anode spread among the community. It attracted groups from Oxford led by Louise Johnson in which Dave Stuart, FRS and Keith Wilson were also involved (J. Appl. Cryst. 16, 28 (1983)) and MRC Cambridge led by Max Perutz (J. Mol. Biol. 175, 159 (1984)).


With the closure of NINA SRF in spring 1977, the construction of the SRS began. On the X-ray beamline, XAFS (station 7.1: Greaves/Hasnain), fibre diffraction (station 7.2: Watson Fuller), topography (station 7.5/7.6, the longest beamline on a synchrotron for some time: Brian Tanner) and X-ray interferometry (station 7.4: Michael Hart) were planned. Watson Fuller who was a Professor of Biophysics at Keele University negotiated a lectureship position jointly funded by Daresbury and Keele and advertised the position so that the individual could take the responsibility for station 7.2 as a station scientist. Fortuitously, John Helliwell decided to apply and was appointed to this important job; he was then able to steer the design of this important station to include both fibre diffraction and protein crystallography. The versatility of the instrument provided evidence for many crystallographic groups to join the UK’s effort of SR structural biology while providing some exciting science related to fibre diffraction (see, e.g. Science 233, 195-197 (1986)).

While line 7 was being commissioned, I started working on a plan to develop beamline 8 where the source properties were much superior to the initial beamlines as the source was at an upstream point of an even-numbered magnet. The beamline was to provide XAFS facilities for dilute systems, particularly biological systems and solution scattering/fibre diffraction. Hugh Huxley, among others, was also involved in detailed specification of the SAXS component of the beamline. The beamline received a real boost with the arrival of the Dutch when NWO signed an agreement in 1982 with SERC to fund this beamline and its two experimental stations.  Things began to move rapidly. In 1983 Joan Bordas arrived as part of the MRC signing a cooperation agreement with the SERC for building a biology support laboratory and another dedicated beamline for SAXS/muscle diffraction.  SERC funded several experimental stations on the first superconducting wavelength shifter where crystallographic station 9.6 was to be installed; this eventually helped solve the foot and mouth disease virus structure (capturing the national television high spot at 9 pm News in 1989; Nature, 337, 709-716 (1989)) and F1-ATPase structure (Nature 371, 621-628 (1994)) that brought the first Nobel prize to the Synchrotron world in 1997 to Sir John Walker from MRC LMB (J. Synchrotron Rad. 6, 809-811 (1999)). My own efforts to combine all of the X-ray techniques (XAFS, SAXS and crystallography) came to fruition at the end of the first decade of the SRS (Biochem Journal, 233, 479 (1986), Biochemistry, 27, 5804 - 5812 (1988) and J Molecular Biol, 225, 811 - 819 (1992)) on iron transport protein, transferrins. This  became the integrated approach of my career since then – fostered by the interdisciplinary environment of the SRS where scientific and technical approaches had no boundaries – the only important aspect of the enterprise was the scientific question.