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Biologische Systeme und Medizin Poster: Mi., 14:00–16:30 M-P207
Biological Small Angle X-ray Scattering at the European Molecular Biology
Laboratory Hamburg - Present State and Future Plans for Petra III
Manfred Roessle 1 , Roy Klaering 2 , Petr Konarev 1 , Uwe Ristau 2 , Bernd
Robrahn 2 , Maxim Pethoukov 1 , Thomas Gehrmann 2 , Stefan Fiedler 2 ,
Christoph Hermes 2 , Dmitri Svergun 1
1 EMBL Hamburg BioSAXS Group Notkestr. 85 D-22603 Hamburg – 2 EMBL Hamburg
X-ray Instrumentation Group Notkestr. 85 D-22603 Hamburg
Small angle X-ray scattering (SAXS) is a versatile tool for structural investigation of
biological molecules in solution, and became a rapidly growing field of research during
the last years. In contrast with other methods in structural biology SAXS allows
to study the overall structure of native particles in solutions and analyze structural
changes in response to variations in external conditions such as temperature, pH etc.
The BioSAXS station X33 at the EMBL Hamburg Outstation was subsequently upgraded
to optimize performance for the scattering studies of macromolecular solutions.
This upgrade includes changes in all components of the station, from major optical
parts to the experimental stage and detector system. This recent technical upgrade of
the BioSAXS station together with advantages in data analysis significantly enhanced
resolution and reliability of structural models provided by the technique. The available
software packages on the BioSAXS station cover all steps in data analysis ranging
from semi-automatic data reduction, data analysis such as Guinier-approximation
(PRIMUS) and indirect Fourier transformation (GNOM) up the ab inito low resolution
model building (DAMMIN and GASBOR). Ab initio model building technique as well
as rigid body modeling allows one to analyze the overall shape of the macromolecule
based only on the scattering data, and taking advantage of already available high
or low resolution structures. Semi-automatic modeling up to completely automatic
rigid body modeling using distance constrains are possible with our present software
packages (DAMMIN, GASBOR, MASSHA, SASREF and BUNCH). This software is
freely available for the academic user community (ATSAS program suite) and widely
used. The new BioSAXS beamline for Petra III will adequately exploit the exceptionally
high brilliance of the Petra-III source to further improve the efficiency of structural
analysis using the small-angle scattering technique accompanying new and fast analysis
methods developed at the EMBL. The BioSAXS station will share the infrastructure
for biological sample preparation and handling with the other EMBL beamlines and
will lead towards a unique environment for cutting edge research and for large scale
analysis of biological macromolecules in combined protein crystallographic - SAXS
studies.
[1] Svergun, D. I. et al. Rep. Progr. Phys. 66, (2003)
[2] Konarev, P. V., et al J. Appl. Crystallogr. 34, (2001)
[3] Vestergaard, B. et al Molecular Cell (2005)
[4] Roessle, M., et al Biomacromolecules 4, (2003)