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Instruments / Technical Area	Publication Details	Published
I22-Small angle scattering & Diffraction	Phase behavior of lysozyme solutions in the liquid–liquid phase coexistence region at high hydrostatic pressures Julian Schulze , Johannes Möller , Jonathan Weiner , Karin Julius , Nico König , Julia Nase , Michael Paulus , Metin Tolan , Roland Winter Physical Chemistry Chemical Physics DOI: 10.1039/C6CP01791F Show Abstract ▼ Abstract: We present results from small-angle X-ray scattering and turbidity measurements on the effect of high hydrostatic pressure on the phase behavior of dense lysozyme solutions in the liquid–liquid phase separation region, and characterize the underlying intermolecular protein–protein interactions as a function of temperature and pressure under charge-screening conditions (0.5 M NaCl). A reentrant liquid–liquid phase separation region is observed at elevated pressures, which may originate in the pressure dependence of the solvent-mediated protein–protein interaction. A temperature-pressure-concentration phase diagram was constructed for highly concentrated lysozyme solutions over a wide range of temperatures, pressures and protein concentrations including the critical region of the liquid–liquid miscibility gap.	May 2016
I22-Small angle scattering & Diffraction	Specific anion effects on the pressure dependence of the protein-protein interaction potential Johannes Moeller , Sebastian Grobelny , Julian Schulze , Andre Steffen , Steffen Bieder , Michael Paulus , Metin Tolan , Roland Winter Physical Chemistry Chemical Physics 16 (16) DOI: 10.1039/c3cp55278k Diamond Proposal Number(s): [7976] Show Abstract ▼ Abstract: We present a study on ion specific effects on the intermolecular interaction potential V(r) of dense protein solutions under high hydrostatic pressure conditions. Small-angle X-ray scattering in combination with a liquid-state theoretical approach was used to determine the effect of structure breaking/making salt anions (Cl−, SO42−, PO43−) on the intermolecular interaction of lysozyme molecules. It was found that besides the Debye–Hückel charge screening effect, reducing the repulsiveness of the interaction potential V(r) at low salt concentrations, a specific ion effect is observed at high salt concentrations for the multivalent kosmotropic anions, which modulates also the pressure dependence of the protein–protein interaction potential. Whereas sulfate and phosphate strongly influence the pressure dependence of V(r), chloride anions do not. The strong structure-making effect of the multivalent anions, dominating for the triply charged PO43−, renders the solution structure less bulk-water-like at high salt concentrations, which leads to an altered behavior of the pressure dependence of V(r). Hence, the particular structural properties of the salt solutions are able to influence the spatial organization and the intermolecular interactions of the proteins, in particular upon compression. These results are of interest for exploring the combined effects of ionic strength, temperature and pressure on the phase behavior of protein solutions, but may also be of relevance for understanding pressure effects on the hydration behavior of biological matter under extreme environmental conditions.	Mar 2014
I22-Small angle scattering & Diffraction	Reentrant liquid-liquid phase separation in protein solutions at elevated hydrostatic pressures Johannes Moeller , Sebastian Grobelny , Julian Schulze , Steffen Bieder , Andre Steffen , Mirko Erlkamp , Michael Paulus , Metin Tolan , Roland Winter Physical Review Letters 112 (2), 028101 DOI: 10.1103/PhysRevLett.112.028101 PMID: 24484044 Diamond Proposal Number(s): [7976, 8604] Show Abstract ▼ Abstract: We present results from small-angle x-ray scattering data on the effect of high pressure on the phase behavior of dense lysozyme solutions in the liquid-liquid phase separation region, and characterize the underlying intermolecular protein-protein interactions as a function of temperature and pressure in this region of phase space. A reentrant liquid-liquid phase separation region has been discovered at elevated pressures, which originates in the pressure dependence of the solvent-mediated protein-protein interactions.	Jan 2014

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