Hydrophobin HFBII in detail: ultrahigh-resolution structure at 0.75 A.

Acta Crystallogr D Biol Crystallogr

Department of Chemistry, University of Joensuu, PO Box 111, 80101 Joensuu, Finland.

Published: April 2006

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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Source
http://dx.doi.org/10.1107/S0907444906000862DOI Listing

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