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Title: Resonant Soft X-Ray Scattering Provides Protein Structure with Chemical Specificity

Abstract

We introduce resonant soft X-ray scattering (RSoXS) as an approach to study the structure of proteins and other biological molecules in solution. Scattering contrast calculations suggest that RSoXS has comparable or even higher sensitivity than hard X-ray scattering because of contrast generated at the absorption edges of constituent elements, such as carbon and oxygen. Here, we demonstrate that working near the carbon edge reveals the envelope function of bovine serum albumin, using scattering volumes of 10-5 μL that are multiple orders of magnitude lower than traditional scattering experiments. Furthermore, tuning the X-ray energy within the carbon absorption edge provides different signatures of the size and shape of the protein by revealing the density of different types of bonding motifs within the protein. The combination of chemical specificity, smaller sample size, and enhanced X-ray contrast will propel RSoXS as a complementary tool to existing techniques for the study of biomolecular structure.

Authors:
; ; ; ; ; ; ORCiD logo;
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Science Foundation (NSF); National Institutes of Health (NIH)
OSTI Identifier:
1573258
Alternate Identifier(s):
OSTI ID: 1656472
Grant/Contract Number:  
AC02-05CH11231; MRI-1626566; AC02-76SF00515; P41GM103393
Resource Type:
Published Article
Journal Name:
Structure
Additional Journal Information:
Journal Name: Structure Journal Volume: 26 Journal Issue: 11; Journal ID: ISSN 0969-2126
Publisher:
Elsevier
Country of Publication:
United Kingdom
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; protein structure; small-angle scattering; soft x-rays; envelope function; RSoXS; SAXS; NEXAFS

Citation Formats

Ye, Dan, Le, Thinh P., Kuei, Brooke, Zhu, Chenhui, Zwart, Peter H., Wang, Cheng, Gomez, Enrique D., and Gomez, Esther W. Resonant Soft X-Ray Scattering Provides Protein Structure with Chemical Specificity. United Kingdom: N. p., 2018. Web. doi:10.1016/j.str.2018.07.018.
Ye, Dan, Le, Thinh P., Kuei, Brooke, Zhu, Chenhui, Zwart, Peter H., Wang, Cheng, Gomez, Enrique D., & Gomez, Esther W. Resonant Soft X-Ray Scattering Provides Protein Structure with Chemical Specificity. United Kingdom. doi:https://doi.org/10.1016/j.str.2018.07.018
Ye, Dan, Le, Thinh P., Kuei, Brooke, Zhu, Chenhui, Zwart, Peter H., Wang, Cheng, Gomez, Enrique D., and Gomez, Esther W. Thu . "Resonant Soft X-Ray Scattering Provides Protein Structure with Chemical Specificity". United Kingdom. doi:https://doi.org/10.1016/j.str.2018.07.018.
@article{osti_1573258,
title = {Resonant Soft X-Ray Scattering Provides Protein Structure with Chemical Specificity},
author = {Ye, Dan and Le, Thinh P. and Kuei, Brooke and Zhu, Chenhui and Zwart, Peter H. and Wang, Cheng and Gomez, Enrique D. and Gomez, Esther W.},
abstractNote = {We introduce resonant soft X-ray scattering (RSoXS) as an approach to study the structure of proteins and other biological molecules in solution. Scattering contrast calculations suggest that RSoXS has comparable or even higher sensitivity than hard X-ray scattering because of contrast generated at the absorption edges of constituent elements, such as carbon and oxygen. Here, we demonstrate that working near the carbon edge reveals the envelope function of bovine serum albumin, using scattering volumes of 10-5 μL that are multiple orders of magnitude lower than traditional scattering experiments. Furthermore, tuning the X-ray energy within the carbon absorption edge provides different signatures of the size and shape of the protein by revealing the density of different types of bonding motifs within the protein. The combination of chemical specificity, smaller sample size, and enhanced X-ray contrast will propel RSoXS as a complementary tool to existing techniques for the study of biomolecular structure.},
doi = {10.1016/j.str.2018.07.018},
journal = {Structure},
number = 11,
volume = 26,
place = {United Kingdom},
year = {2018},
month = {11}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
DOI: https://doi.org/10.1016/j.str.2018.07.018

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Cited by: 2 works
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