Siliconized glass circular cover slides

Dynamic light-scattering (DLS) measurements were performed using a NaBiTec GmbH setup comprising a SpectroSize 302 (Molecular Dimensions) in combination with an S6D microscope (Leica). The purified protein sample was concentrated to 10 mg/mL as described earlier was illuminated in a 2 μl hanging drop using a 24-well crystallization plate (VDX Greased Plate, Hampton Research) covered with siliconized-glass circular cover slides (22 mm; Hampton Research). The well itself was filled with 400 μl SEC running buffer. Prior to the measurement, the protein solution was centrifuged at 18000 ×g, 30 min, 4°C to remove possible dust and other suspended particles. All measurements were done at 20°C. Ten consecutive measurements, each with an integration time of 20 s, were averaged. Hydrodynamic size of the particles was estimated with the instrument software using the following parameters: refractive index 1.33, viscosity 1.006, shape factor 1.0 and hydrated shell 0.2 nm.

Dynamic light-scattering (DLS) measurements were performed using a NaBiTec GmbH setup comprising a SpectroSize 302 (Molecular Dimensions) in combination with an S6D microscope (Leica). The purified protein sample (concentrated to 8 mg ml⁻¹ as described above) was illuminated in a 3 µl hanging drop using a 24-well crystallization plate (VDX Greased Plate, Hampton Research) covered with siliconized-glass circular cover slides (22 mm; Hampton Research). The well itself was filled with 600 µl SEC running buffer. Prior to the measurement, the protein solution was centrifuged (1000g, 30 min, 4°C) to remove possible dust particles. During the measurement, the temperature was set to 20°C. Ten consecutive measurements, each with an integration time of 20 s, were averaged. An estimate of the hydrodynamic size was obtained with the instrument software using the following parameters: refractive index 1.33, viscosity 1.006, shape factor 1.0, hydrated shell 0.2 nm.