Use of dynamic light scattering to assess crystallizability of macromolecules and macromolecular assemblies  Adrian R Ferré-D'Amaré, Stephen K Burley  Structure  Volume 2, Issue 5, Pages 357-359 (May 1994) DOI: 10.1016/S0969-2126(00)00037-X

Figure 1 Distribution of apparent molecular weight determined by DLS for seven protein–DNA complexes. Success achieved in crystallizing each complex is indicated. (a) Complete USF protein and the carboxy-terminal truncated protein USF(1–260). (b) USF protein with amino-terminal deletion [USF(196–310)] and with a further carboxy-terminal deletion [USF(196–260)]. (c) Carboxy-terminal deletion of Max(1–113) and two further amino- terminal deletions [Max (11–113) and Max(22–113)]. All proteins were mixed with stoichiometric amounts of duplex oligonucleotide with the appropriate binding site. The measurements were performed using a DynaPro-801 Molecular Sizing Instrument (Protein Solutions, Inc., Charlottesville, VA) with the protein– DNA complexes at concentrations of 1–3 mg ml −1 in 100 mM KCl, 10 mM Hepes-KOH pH 7.5, (and 5 mM dithiothreitol for proteins with cysteines). These data underscore the difference between DLS and gel filtration, which cannot distinguish between broad unimodal and narrow unimodal size distributions that do crystallize. Structure 1994 2, 357-359DOI: (10.1016/S0969-2126(00)00037-X)