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Figure 7
SAXS experiments combined with in situ DLS data collection to monitor particle size and to verify the SAXS data quality in the newly designed SEU. Scattering data of three standard proteins covering a wide molecular weight range are displayed. (a) Scattering intensities of RNase A (10 mg ml−1), BSA (8 mg ml−1) and apoferritin (5 mg ml−1) were compared with the respective entries in the BioSAXS database SASBDB. The accompanying fit curve for each protein (black lines) calculated from the respective high-resolution structures is shown as well. The high similarity of the recorded SAXS data compared with previously collected data deposited in the database verifies that SAXS and DLS data can be collected in parallel applying the newly implemented SEU. The scattering intensity values of each protein are displaced vertically for clarity. (b) Averaged ACFs of the DLS data collected in parallel for the samples shown in Fig. 5[link](a).

Journal logoJOURNAL OF
SYNCHROTRON
RADIATION
ISSN: 1600-5775
Volume 25| Part 2| March 2018| Pages 361-372
https://doi.org/10.1107/S1600577517017568
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