Anomalous x-ray scattering from terbium-labeled parvalbumin in solution.

Abstract:

:We have used anomalous small-angle x-ray scattering as a structural probe for solutions of rabbit parvalbumin labeled with terbium. This technique makes use of the large changes in the terbium scattering factor that occur when the x-ray energy is tuned around an L3 absorption edge of this heavy-atom label. These changes in scattering result in changes in the small-angle scattering curve of the labeled protein as a whole, which can then be analyzed to derive structural information concerning the distribution of labels in the protein. Based on a Gaussian model for the protein electron density, the mean distance from the terbiums to the protein center of mass is determined to be 13.2 A and is consistent with crystallographic results. Our results demonstrate the usefulness of terbium as an anomalous scattering label and provide criteria to help establish anomalous scattering as a reliable structural technique for proteins in solution.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Miake-Lye RC,Doniach S,Hodgson KO

doi

10.1016/S0006-3495(83)84440-3

subject

Has Abstract

pub_date

1983-03-01 00:00:00

pages

287-92

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(83)84440-3

journal_volume

41

pub_type

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