Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBI

9Citations
Citations of this article
26Readers
Mendeley users who have this article in their library.

This article is free to access.

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 P61 (or P65), with unit-cell parameters a = b = 45.9, c = 307.2 Å. The HFBI used in the crystallization experiments was purified from fungal cell walls. © 2004 International Union of Crystallography.

Cite

CITATION STYLE

APA

Askolin, S., Turkenburg, J. P., Tenkanen, M., Uotila, S., Wilson, K. S., Penttilä, M., & Visuri, K. (2004). Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBI. Acta Crystallographica Section D: Biological Crystallography, 60(10), 1903–1905. https://doi.org/10.1107/S0907444904019754

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free