Aarhus, Denmark
3 - 6 October 2001









Updated: 30 April 2001
 Summary 

Purpose

The main aim of the BLIS workshop is to describe the latest theory and practice of low- and intermediate- energy synchrotron radiation (SR) techniques that have become popular in biology research. Unlike large expensive high-energy storage rings designed to produce x-rays (>1 keV) for protein crystallography, low-energy storage rings such as ASTRID produce radiation optimised for the study of molecular electronic transitions (1-100 eV) and makes available a host of photobiology techniques. Topic sessions will cover a variety of  techniques over a wide range of applications at the molecular, cellular and organism level. The fusion of biological and physical sciences at the workshop is expected to encourage cross-disciplinary as well as inter-technique dialogue among biologists, chemists, engineers and physicists. A vital aspect of the BLIS workshop is the inspiration of young scientists to pursue research in the field of SR, its related technologies and applications.  To this end we plan to fund some student attendees. 

 The major part of the workshop will be dedicated to lectures by experts on SR based techniques and biological applications. Additionally, afternoon sessions are reserved for poster and oral presentations by attendees on related topics. There will also be the opportunity to gain 'hands-on' experience, performing experiments on their own samples
 using the CD, XM and GBS facilities. Please contact the organisers to discuss specimen requirements and machine specifications as soon as possible. 

Techniques

 Circular Dichroism (CD) spectroscopy: CD takes advantage of the intrinsic chirality of nature using the differential absorption of left- and right-circularly polarised light to determine secondary structure content of proteins and nucleic acids. Protein molecule stability and conformational changes can be studied as a function of environment as well as folding and unfolding processes under normal and abnormal physiological conditions. The SR provided by ASTRID permits new information on molecular structure to be gathered at lower wavelengths, higher data rates and increased signal-to-noise ratios; thereby allowing more  extensive experiments to be performed, such as stop-flow. Attendees will be given the opportunity to use SR CD on ASTRID during the workshop. Contact John Kenney for more information.  

 Fourier Transform Infrared (FT IR) Spectroscopy: FT IR is also used to study the secondary structure of proteins, which can be interpreted from their characteristic infrared spectra. FT IR data is often used to complement the UV data of CD. Low energy SR facilities, such as ASTRID, are ideal sources of tuneable IR to get clean data, especially for applications requiring high intensity, such as FT IR microscopy.  

 Fluorescence Spectroscopy: Fluorescence is used to study biomolecular dynamics on a very short time scale. It can also be coupled with other techniques, e.g., CD, to further elucidate molecular structure. Pulsed sources of SR in the visible, UV and VUV can be used to probe the molecular behaviour on very short time scales.  

 X-ray Microscopy (XM): XM takes advantage of the so-called water window, accessible using SR, to image thick (up to 10 µm) hydrated biological specimens with high contrast. High-resolution (20-50 nm) images can be obtained of whole cells in solution without chemical fixation, staining or drying. Cells are alive up until the moment the image is taken. Attendees will be given the opportunity to use the transmission XM on ASTRID during the workshop. Contact Joanna Abraham-Peskir for more information.  

 Medical tomography: Tomography on a microscopic scale (with µm-level resolution) with is only possible using SR. The technique is particularly suitable for characterising pathological cell structure in bone. 

 Gas-phase Biomolecule Spectroscopy (GBS): The electrostatic storage ring ELISA can store large biomolecule ions for gas-phase experiments. This unique facility provides the opportunity to make rapid lifetime studies of biomolecules to study conformational changes and should provide valuable information on protein dynamics. Attendees interested in GBS on ELISA and especially to get experience with the technique during the workshop should contact Søren Pape Møller for more information.