6lng

Rapid crystallization of streptavidin using charged peptides

spinqualitylabelsall models 6lng, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lng is a 6 chain structure with sequence from Streptomyces avidinii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8000015Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SAV_STRAV The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMed We utilized electrostatic interaction to induce rapid crystallization of streptavidin. Simply mixing streptavidins possessing either a positively or negatively charged peptide at their C-terminus generated diffraction-quality crystals in a few hours. We modified the streptavidin crystals with fluorescent molecules using biotin, demonstrating the concept of protein crystals as functional biomaterials. Genetically fused charged peptides induce rapid crystallization of proteins.,Minamihata K, Tsukamoto K, Adachi M, Shimizu R, Mishina M, Kuroki R, Nagamune T Chem Commun (Camb). 2020 Mar 5. doi: 10.1039/c9cc09529b. PMID:32134050 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Avidin 3D structures

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