5JD2

SFX structure of corestreptavidin-selenobiotin complex

Summary for 5JD2

• Entry DOI: 10.2210/pdb5jd2/pdb
• Descriptor: Streptavidin, 5-[(3aS,4S,6aR)-2-oxohexahydro-1H-selenopheno[3,4-d]imidazol-4-yl]pentanoic acid (3 entities in total)
• Functional Keywords: sad, sfx, fel, streptavidin, biotin binding protein
• Biological source: Streptomyces avidinii
• Total number of polymer chains: 4
• Total formula weight: 51939.85

Authors

DeMirci, H.,Hunter, M.S.,Boutet, S. (deposition date: 2016-04-15, release date: 2016-11-16, Last modification date: 2024-03-06)

Primary citation

Hunter, M.S.,Yoon, C.H.,DeMirci, H.,Sierra, R.G.,Dao, E.H.,Ahmadi, R.,Aksit, F.,Aquila, A.L.,Ciftci, H.,Guillet, S.,Hayes, M.J.,Lane, T.J.,Liang, M.,Lundstrom, U.,Koglin, J.E.,Mgbam, P.,Rao, Y.,Zhang, L.,Wakatsuki, S.,Holton, J.M.,Boutet, S.
Selenium single-wavelength anomalous diffraction de novo phasing using an X-ray-free electron laser.
Nat Commun, 7:13388-13388, 2016

PubMed Abstract: Structural information about biological macromolecules near the atomic scale provides important insight into the functions of these molecules. To date, X-ray crystallography has been the predominant method used for macromolecular structure determination. However, challenges exist when solving structures with X-rays, including the phase problem and radiation damage. X-ray-free electron lasers (X-ray FELs) have enabled collection of diffraction information before the onset of radiation damage, yet the majority of structures solved at X-ray FELs have been phased using external information via molecular replacement. De novo phasing at X-ray FELs has proven challenging due in part to per-pulse variations in intensity and wavelength. Here we report the solution of a selenobiotinyl-streptavidin structure using phases obtained by the anomalous diffraction of selenium measured at a single wavelength (Se-SAD) at the Linac Coherent Light Source. Our results demonstrate Se-SAD, routinely employed at synchrotrons for novel structure determination, is now possible at X-ray FELs.

PubMed: 27811937
DOI: 10.1038/ncomms13388

Experimental method

X-RAY DIFFRACTION (1.9 Å)