Data and scripts from: Temperature-dependent interactions explain normal and inverted solubility in a γD-crystallin mutant

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  • Protein crystal production is a major bottleneck in the structural characterisation of proteins. To advance beyond large-scale screening, rational strategies for protein crystallization are crucial. Understanding how chemical anisotropy (or patchiness) of the protein surface due to the variety of amino acid side chains in contact with solvent, contributes to protein-protein contact formation in the crystal lattice is a major obstacle to predicting and optimising crystallization. The relative scarcity of sophisticated theoretical models that include sufficient detail to link collective behaviour, captured in protein phase diagrams, and molecular level details, determined from high-resolution structural information is a further barrier. Here we present two crystals structures for the P23T+R36S mutant of γD-crystallin, each with opposite solubility behaviour -- one melts when heated, the other when cooled. When combined with the protein phase diagram and a tailored patchy particle model we show that a single temperature dependent interaction is sufficient to stabilise the inverted solubility crystal. This contact, at the P23T substitution site, relates to a genetic cataract and reveals at a molecular level, the origin of the lowered and retrograde solubility of the protein. Our results show that the approach employed here may present an alternative strategy for the rationalization of protein crystallization. ... [Read More]

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  • Khan, A., James, S., Quinn, M., Altan, I., Charbonneau, P., & McManus, J. (2019). Data and scripts from: temperature-dependent interactions explain normal and inverted solubility in a γD-crystallin mutant. Duke Digital Repository. https://doi.org/10.7924/r49w0dx6s
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  • 10.7924/r49w0dx6s
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  • ark:/87924/r49w0dx6s
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  • Khan, A. R., James, S., Quinn, M. K., Altan, I., Charbonneau, P., & McManus, J. J. (2019). Temperature-Dependent interactions EXPLAIN normal and INVERTED solubility in a γd-crystallin mutant. Biophysical Journal, 117(5), 930-937. doi:10.1016/j.bpj.2019.07.019.  https://doi.org/10.1016/j.bpj.2019.07.019
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  • Data and scripts from: Temperature-dependent interactions explain normal and inverted solubility in a γD-crystallin mutant
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Thumbnail Title Date Uploaded Visibility Actions
file details Readme.txt 2019-07-17 Public Download
file details 2a_view.py 2019-07-17 Public Download
file details 2c_view.py 2019-07-17 Public Download
file details DBI_exp.dat 2019-07-17 Public Download
file details DBN_exp.dat 2019-07-17 Public Download
file details expData.dat 2019-07-17 Public Download
file details interX.m 2019-07-17 Public Download
file details 2b_view.py 2019-07-17 Public Download
file details 3a_view.py 2019-07-17 Public Download
file details DBI_sim.dat 2019-07-17 Public Download

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