Related Experiment Video
Updated: Aug 22, 2026

Recombinant Production And Purification of Hydrophobin SC16 From Escherichia coli And Monitoring of Its Self-Assembly Using Fluorescence Assays
Published on: June 5, 2026
Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBI
Sanna Askolin1, Johan P Turkenburg, Maija Tenkanen
1VTT Biotechnology, FIN-02044 VTT, Finland. sanna.askolin@finnzymes.fi
Abstract:
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.

