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Updated: Aug 9, 2026
Recombinant Production And Purification of Hydrophobin SC16 From Escherichia coli And Monitoring of Its Self-Assembly Using Fluorescence Assays
Published on: June 5, 2026
Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A
Johanna Hakanpää1, Markus Linder, Alexander Popov
1Department of Chemistry, University of Joensuu, PO Box 111, 80101 Joensuu, Finland. johanna.hakanpaa@joensuu.fi
Abstract:
Hydrophobins are small proteins secreted by filamentous fungi that have a unique ability to spontaneously form amphiphilic layers. Hydrophobins have only recently been structurally characterized through the first crystal structure determination of a protein of this class, Trichoderma reesei hydrophobin HFBII [Hakanpää, Paananen et al. (2004), J. Biol. Chem. 279, 534-539]. The resolution of the HFBII structure has now been extended to an ultrahigh resolution of 0.75 A. The structure was refined conventionally and multipole refinement has been initiated. The ultrahigh-resolution structure is analyzed here in detail and comparison is made to the previous atomic resolution structure of the same protein as well as to other ultrahigh-resolution structures found in the Protein Data Bank.
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