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K-edge anomalous SAXS for protein solution structure modeling

Authors :
Karman Virk
Kento Yonezawa
Komal Choukate
Lucky Singh
Nobutaka Shimizu
Barnali Chaudhuri
Source :
Acta Crystallographica Section D Structural Biology. 78:204-211
Publication Year :
2022
Publisher :
International Union of Crystallography (IUCr), 2022.

Abstract

K-edge anomalous SAXS intensity was measured from a small, dimeric, partly unstructured protein segment of myosin X by using cupric ions bound to its C-terminal polyhistidine tags. Energy-dependent anomalous SAXS can provide key location-specific information about metal-labeled protein structures in solution that cannot be obtained from routine SAXS analysis. However, anomalous SAXS is seldom used for protein research due to practical difficulties, such as a lack of generic multivalent metal-binding tags and the challenges of measuring weak anomalous signal at the metal absorption edge. This pilot feasibility study suggests that weak K-edge anomalous SAXS signal can be obtained from transition metals bound to terminally located histidine tags of small proteins. The measured anomalous signal can provide information about the distribution of all metal–protein distances in the complex. Such an anomalous SAXS signal can assist in the modeling and validation of structured or unstructured proteins in solution and may potentially become a new addition to the repertoire of techniques in integrative structural biology.

Details

ISSN :
20597983
Volume :
78
Database :
OpenAIRE
Journal :
Acta Crystallographica Section D Structural Biology
Accession number :
edsair.doi.dedup.....85aa44c78856a49778e5b6355b5019cd
Full Text :
https://doi.org/10.1107/s205979832101247x