Abstract
X-ray diffraction with synchrotron radiation (SR) has revealed the atomic structures of numerous biological macromolecules including proteins and protein complexes, nucleic acids and their protein complexes, viruses, membrane proteins and drug targets. The bright SR X-ray beam with its small divergence has made the study of weakly diffracting crystals of large biological molecules possible. The ability to tune the wavelength of the SR beam to the absorption edge of certain elements has allowed anomalous scattering to be exploited for phase determination. We review the developments at synchrotron sources and beamlines from the early days to the present time, and discuss the significance of the results in providing a deeper understanding of the biological function, the design of new therapeutic molecules and time-resolved studies of dynamic events using pump–probe techniques. Radiation damage, a problem with bright X-ray sources, has been partially alleviated by collecting data at low temperature (100 K) but work is ongoing. In the most recent development, free electron laser sources can offer a peak brightness of hard X-rays approximately 10 8 times brighter than that achieved at SR sources. We describe briefly how early experiments at FLASH and Linear Coherent Light Source have shown exciting possibilities for the future.
Highlights
X-ray diffraction with synchrotron radiation (SR) has revealed the atomic structures of numerous biological macromolecules including proteins and protein complexes, nucleic acids and their protein complexes, viruses, membrane proteins and drug targets
In 1970, the first experimental use of SR in biology was made by Rosenbaum, Witz and Holmes at the Deutsches Elektronen Synchrotron (DESY), Hamburg, Germany, where it was shown that diffraction from a muscle fibre could be recorded with very much shorter exposure times than with a laboratory-based X-ray source (Rosenbaum et al 1971)
From images collected at Linear Coherent Light Source (LCLS) with wavelength 6.9 Å, pulse length 70 fs and 1.6 × 1010 photons mm−2 delivered to the sample, a two-dimensional reconstructed image of 16 nm resolution was obtained showing the viral shell of protein and phospholipids and some internal structure
Summary
We identify advances in modern-day macromolecular crystallography (MX) that have been made possible using synchrotron radiation (SR). There was a demand for stable storage rings dedicated to the production of X-rays and this led to the construction of second-generation sources. The synchrotron radiation source (SRS) at Daresbury, UK, commissioned in 1981, was the first such facility to be built with the MX beamline 7.2 (Helliwell et al 1982), and. Other first-generation accelerators such as LURE, Cornell High Energy Synchrotron Source (CHESS, Cornell, NY), SSRL and DESY were upgraded for production of SR (reviewed by Helliwell 1984). In the mid-1990s, third-generation sources with lower source sizes and lower emittance were built to meet this need The first such sources with MX beamlines were the European Synchrotron Radiation Facility (ESRF, Grenoble, France; 1994), the Advanced Photon Source (APS, Argonne, IL; 1996) and Super Photon ring 8 (SPring, Harima, Japan; 1997). In 1997, on the decommissioning of the BESSY I synchrotron, the initiative of some visionary scientists led to an arrangement to ship components to the Middle East to found SESAME (Synchrotron-light for Experimental Science and Applications in the Middle East), a synchrotron being built by a consortium of seven countries (Bahrain, Egypt, Israel, Jordan, Pakistan, Palestine and Turkey with several others about to join), as a facility for science and a focus for peaceful cooperation
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