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Open Dataset XSJFSD8I

Green Fluorescent Protein (GFP) Supercharged -29 with Chloride Salts

Abstract

Green Fluorescent Protein (GFP) is a ubiquitous protein for structural biology. Super stable versions of GFP have been created. Super charged variants were created based on the super stable variant and SAXS studies pursued, in a paper titled "SAXS/SANS on Supercharged Proteins Reveals Residue-Specific Modifications of the Hydration Shell" authored by Henry S Kim et al in Biophys J. 2016. This is a follow-on study of the -29 supercharged variant where more conditions were collected. Four concentrations of -29 super charged GFP (4, 6, 8, 10mg/mL) were collected in LiCl, NaCl, KCl, RbCl and CsCl. Each salt was added to the GFP solution in three concentrations at (10, 100 and 500 mM). Thus 60 experiments were conducted in total. Protein concentration series were corrected for radiation damage and concentration dependence. Thus, the total experiments deposited here are 15 as protein concentrations are bundled into one concentration. Because GFP is positively supercharged and the varying cation from the salt will be repelled from the protein surface adjusting the contrast of the hydration layer around the protein relative to the bulk solution. The hope is this study will provide a way to develop better models of the hydration layer.

Experimental description

Four concentrations of -29 super charged GFP (4, 6, 8, 10mg/mL) were collected in LiCl, NaCl, KCl, RbCl and CsCl. Each salt was added to the GFP solution in three concentrations at (10, 100 and 500 mM). Protein concentration series were corrected for radiation damage and concentration dependence. Thus, the total experiments deposited here are 15 as protein concentrations are bundled into one concentration.

File description

File names are labelled in the following manner SuperChargeValance_SaltConcentrationmM_SaltType.dat. So the example file name 29_500mMKCl.dat represents the -29 Super charged GFP at 500mM KCl.

Created

2021-03-08

Published

2022-08-16

Data collection technique

HT-SAXS

Journal DOI

Source

Beamline

Wavelength

Sample to Detector Distance

Submitting Author

Greg Hura

Lawrence Berkeley National Laboratory, The SIBYLS Beamline

United States of America

[email protected]

Collaborators

Jan Bierma, Tad Ogorzalek

Project Leader

Greg Hura

[email protected]


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Complete Set of SAS Data Files

The complete SAS dataset is downloadable as a zip file.

Individual SAS Data Files (total 1)

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Supplemental Data and Supporting Materials (total 0)

These data and materials may include X-ray crystal structure coordinates, multi-angle light scattering data, .etc. It may also include additional details or methods pertaining to the SAXS experiments, or the researcher's interpretations of the results.

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SAXS Similarity SAXS FrameSlice

Sample:

  • Macromolecule 1: GFP
    • Sample Full Name: Green Fluorescent Protein
    • Sample Type: Protein
    • Source Organism:
    • Source Organism NCBI Taxonomy ID:
    • Expression System:
    • Expression NCBI Taxonomy ID:
    • Sequence or Chemical Formula: