Research on liquid-liquid phase separation (LLPS) and cellular condensates is on the rise in both academia and industry. As condensates such as the nucleolus, P bodies, and stress granules are further investigated and determined to be an essential underlying method of membrane-less cellular organization, more experiments on them need to be done more efficiently (Hyman et al., 2014; Banani et al., 2017). Many proteins and/or simple mixtures of biopolymers such as protein and RNA are necessary and sufficient to drive LLPS in vitro (Zhang et al., 2015; Feric et al., 2016). Detailed analysis of these protein mixtures must be undertaken to uncover what drives the formation of a phase separated condensates. Indeed, the construction of phase diagrams from experimental measurements provides critical insight into the thermodynamic constraints governing LLPS. Such phase diagrams may be constructed along orthogonal axes such as salt v. protein concentration, RNA v. protein concentration, and temperature v. protein concentration.

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Static right-angle light scattering (SRALS) is a quantitative measurement of the size of proteins or higher order assemblies present in solution. Thus, SRALS is a powerful experimental technique

for measuring LLPS in vitro because sharp increases in scattering intensity are reflective of the

formation of phase separated condensates in the sample of interest. Additionally, the intensity of scattering is proportional to the size and number of condensates. Current limitations of SRALS, specifically the set up within the Pappu Lab, which is representative of standard academic laboratory environments, are throughput and sample volume requirements. To measure scattering with the current experimental set up, samples must be measured one by one, and each sample must be at least 150 μL in volume. The time and material costs of these experiments are enormous especially considering that over 100 data points are generally required to accurately construct a phase diagram. These limitations to SRALS are also faced in private research environments and can expand into industry. Thus, the market for a high throughput solution for measuring temperature dependent phase separation by SRALS involves both private and public researchers on an international scale. Further, since SRALS can also be used to measure many other biophysical phenomena such as neurodegenerative protein aggregation, protein stability, and synthetic polymer thermodynamics, adaptable, high throughput adaptations to SRALS could reach far beyond the world of temperature-dependent LLPS (Posey et al., 2018; Senisterra et al., 2006; Terao & Mays, 2004).