Fayter, Alice E. R., Huband, Steven and Gibson, Matthew I. (2020) Data for X-ray diffraction to probe the kinetics of ice recrystallization inhibition. [Dataset]

	Archive (ZIP) (Zip archive) Data.zip - Published Version Available under License Creative Commons Attribution 4.0. Download (28Mb)
	Plain Text (Readme file) Readme.txt - Published Version Available under License Creative Commons Attribution 4.0. Download (490b)

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Abstract

Understanding the nucleation and growth of ice is crucial in fields ranging from infrastructure maintenance, to the environment, and to preserving biologics in the cold chain. Ice binding and antifreeze proteins are potent ice recrystallization inhibitors (IRI), and synthetic materials that mimic this function have emerged, which may find use in biotechnology. To evaluate IRI activity, optical microscopy tools are typically used to monitor ice grain size either by end-point measurements or as a function of time. However, these methods provide 2-dimensional information and image analysis is required to extract the data. Here we explore using wide angle X-ray scattering (WAXS/X-ray powder diffraction (XRD)) to interrogate 100's of ice crystals in 3-dimensions as a function of time. Due to the random organization of the ice crystals in the frozen sample, the number of orientations measured by XRD is proportional to the number of ice crystals, which can be measured as a function of time. This method was used to evaluate the activity for a panel of known IRI active compounds, and shows strong agreement with results obtained from cryo-microscopy, as well as being advantageous in that time-dependent ice growth is easily extracted. Diffraction analysis also confirmed, by comparing the obtained diffraction patterns of both ice binding and non-binding additives, that the observed hexagonal ice diffraction patterns obtained cannot be used to determine which crystal faces are being bound. This method may help in the discovery of new IRI active materials as well as enabling kinetic analysis of ice growth.

Item Type:	Dataset
Subjects:	Q Science > QA Mathematics Q Science > QD Chemistry Q Science > QP Physiology T Technology > TA Engineering (General). Civil engineering (General) T Technology > TN Mining engineering. Metallurgy T Technology > TP Chemical technology
Divisions:	Faculty of Science, Engineering and Medicine > Science > Chemistry
Type of Data:	Experimental data
Library of Congress Subject Headings (LCSH):	X-ray diffraction imaging, Recrystallization (Metallurgy), Dynamics, Nucleation, Antifreeze proteins, Biotechnology
Publisher:	University of Warwick, Department of Chemistry
Official Date:	15 April 2020
Dates:	Date Event 15 April 2020 Published
Status:	Not Peer Reviewed
Publication Status:	Published
Media of Output (format):	.dat .pdf .txt
Access rights to Published version:	Open Access (Creative Commons)
Copyright Holders:	University of Warwick
Description:	Data record consists of a zip archive containing subfolders, raw data in .dat format, a PDF documentation file summarising the raw XFAS data, and an accompanying readme file. Data files are named and organised according to the corresponding figure in the related paper. Further information on specific data files can be found in the accompanying readme file.
Date of first compliant deposit:	16 April 2020
Date of first compliant Open Access:	16 April 2020
RIOXX Funder/Project Grant:	Project/Grant ID RIOXX Funder Name Funder ID CRYOMAT 638661 European Research Council http://dx.doi.org/10.13039/501100000781 R1\191037 Royal Society http://dx.doi.org/10.13039/501100000288 UNSPECIFIED Royal Society http://dx.doi.org/10.13039/501100000288
Related URLs:	Related item in WRAP Other
Contributors:	Contribution Name Contributor ID Depositor Gibson, Matthew I. 32015

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