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 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.
Original language | English |
---|---|
Pages (from-to) | 356-367 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 62 |
Issue number | 4 |
DOIs | |
Publication status | Published - 2006 |
MoE publication type | A1 Journal article-refereed |
Keywords
- proteins
- hydrophobins
- filamentous fungi
- Trichoderma reesei
- crystallization