SANS and USANS of alpha-synuclein protein mutations
In this work, we hope to explore the relationship between surface chemistry and aggregate formation for a series of alpha;-synuclein mutations, by measuring their structural properties as a function of concentration and carefully chosen salt additives. This study aims to expand on recent work conducted on SANS2D (ISIS) and will involve time and temperature-controlled SANS measurements, to not only determine the internal structure or structures present in each system, but also the key factors governing the aggregation process. In addition, we would like to perform USANS measurements that will serve to characterise large scale aggregation and structures within these systems.
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Download DataThe recommended format for citing this dataset in a research publication is in the following format:
Thomas M. McCoy; ARMSTRONG Alexander; KAMINSKI Gabi; MARTEL Anne; ROUTH Alexander and Amberley D. Stephens. (2020). SANS and USANS of alpha-synuclein protein mutations. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-974
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