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DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
DAMMIF, an enhanced and significantly faster implementation of the ab-initio shape-determination program DAMMIN for small-angle scattering data, is presented.
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New developments in the ATSAS program package for small-angle scattering data analysis
We present new developments and amendments to the ATSAS package (version 2.4) for processing and analysis of isotropic small-angle scattering data. Expand
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ATSAS 2.8: a comprehensive data analysis suite for small-angle scattering from macromolecular solutions
Developments and improvements of the ATSAS software suite (versions 2.5–2.8) for analysis of small-angle scattering data of biological macromolecules or nanoparticles are described. Expand
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Versatile sample environments and automation for biological solution X-ray scattering experiments at the P12 beamline (PETRA III, DESY)
An integrated environment for biological small-angle X-ray scattering (BioSAXS) at the high-brilliance P12 synchrotron beamline of the EMBL (DESY, Hamburg) allows for a broad range of solution scattering experiments. Expand
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Correlation Map, a goodness-of-fit test for one-dimensional X-ray scattering spectra
Assessing similarity between data sets with the reduced χ2 test requires the estimation of experimental errors, which, if incorrect, may render statistical comparisons invalid. We report aExpand
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The Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain
Homodimerization is an essential step for membrane type 1 matrix metalloproteinase (MT1-MMP) to activate proMMP-2 and to degrade collagen on the cell surface. To uncover the molecular basis of theExpand
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Automated sample-changing robot for solution scattering experiments at the EMBL Hamburg SAXS station X33
An automated sample changer for small-angle X-ray scattering (SAXS) on protein in solution is reported. Expand
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Automated Pipeline for Purification, Biophysical and X-Ray Analysis of Biomacromolecular Solutions
Small angle X-ray scattering (SAXS), an increasingly popular method for structural analysis of biological macromolecules in solution, is often hampered by inherent sample polydispersity. Expand
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ISPyB for BioSAXS, the gateway to user autonomy in solution scattering experiments
The ISPyB information-management system for crystallography has been adapted to include data from small-angle X-ray scattering of macromolecules in solution experiments. Expand
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Consensus Bayesian assessment of protein molecular mass from solution X-ray scattering data
Molecular mass (MM) is one of the key structural parameters obtained by small-angle X-ray scattering (SAXS) of proteins in solution and is used to assess the sample quality, oligomeric compositionExpand
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