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 Jjournal_title
Biophysical journalauthors
Miake-Lye RC,Doniach S,Hodgson KOdoi
10.1016/S0006-3495(83)84440-3subject
Has Abstractpub_date
1983-03-01 00:00:00pages
287-92issue
3eissn
0006-3495issn
1542-0086pii
S0006-3495(83)84440-3journal_volume
41pub_type
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