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. Author manuscript; available in PMC: 2011 May 14.
Published in final edited form as: Nat Methods. 2009 Jul 20;6(8):606–612. doi: 10.1038/nmeth.1353

Figure 2.

Figure 2

SAXS analysis provides feedback on challenging samples that are polydisperse or inhomogeneous. (a) PF0230 and PF1548 were mixtures by native gel electrophoresis. Overlaying the SAXS-predicted PF0230 envelope with a close homolog (PDB 2CWE) revealed consistency to the homolog dimer with additional density indicating a larger species. (b) SAXS results directly discerned aggregation based on low angle Guinier regions (insert) for three protein samples PF0418 (red), PF1733 (blue) and PF1281 (green). Features (oscillations) in the SAXS scattering curve for PF0418 and PF1281 suggest that small adjustments in sample preparation may yield workable data, e.g. PF1281 was markedly improved after passing through a filter (purple). (c) Probable multimers may be identified when atomic resolution results are available of the protein or a homolog. Here, multimers in crystal lattices (PF0094 homolog PDB 1J08, PF0380 PDB 1VK1, PF0930 homolog PDB 1V7L, and PF1090 PDB 1SJ1) are used to identify a best fit to the SAXS data.