Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBI.
Hydrophobins are fungal proteins that are capable of altering the hydrophobicity of surfaces by self-assembly at hydrophilic-hydrophobic interfaces. Here, the growth of hydrophobin crystals suitable for X-ray crystallography is reported. The hydrophobin HFBI from Trichoderma reesei was crystallized by vapour diffusion in hanging drops in 30% PEG 4000, 0.1 M sodium citrate pH 4.3 buffer containing 0.2 M ammonium acetate and CYMAL-5 detergent (initial concentration of 2.4 mM). HFBI crystals are hexagonal and belong to space group P6(1) (or P6(5)), with unit-cell parameters a = b = 45.9, c = 307.2 A. The HFBI used in the crystallization experiments was purified from fungal cell walls.
Askolin
Sanna
S
VTT Biotechnology, FIN-02044 VTT, Finland. sanna.askolin@finnzymes.fi
Turkenburg
Johan P
JP
Tenkanen
Maija
M
Uotila
Sinikka
S
Wilson
Keith S
KS
Penttilä
Merja
M
Visuri
Kalevi
K
D003460:Crystallization; D018360:Crystallography, X-Ray; D004058:Diffusion; D005656:Fungal Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D013696:Temperature; D014242:Trichoderma / Q000737:chemistry*; D014961:X-Ray Diffraction
D005656:Fungal Proteins