Virk , Karman and Yonezawa , Kento and Choukate , Komal and Singh , Lucky and Shimizu , Nobutaka and Chaudhuri , Barnali (2022) K-edge anomalous SAXS for protein solution structure modeling. Acta crystallographica. Section D, Structural biology, 78. pp. 204-211. ISSN 2059-7983
Full text not available from this repository. (Request a copy)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.
| Item Type: | Article |
|---|---|
| Additional Information: | The copyright of this article belongs to International Union of Crystallography |
| Uncontrolled Keywords: | SAXS; anomalous scattering; ensemble structure; integrative structural biology; protein structure in solution |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 25 Jul 2022 09:28 |
| Last Modified: | 25 Jul 2022 09:28 |
| URI: | http://crdd.osdd.net/open/id/eprint/3005 |
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