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
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