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 Å. 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.
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Publication status||Published - 2006|
|MoE publication type||A1 Journal article-refereed|
- filamentous fungi
- Trichoderma reesei
Hakanpää, J., Linder, M., Popov, A., Schmidt, A., & Rouvinen, J. (2006). Hydrophobin HFBII in detail: Ultrahigh-resolution structure at 0.75 Å. Acta Crystallographica Section D: Biological Crystallography, 62(4), 356-367. https://doi.org/10.1107/S0907444906000862