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

Sanna Askolin; Johan P. Turkenburg; Maija Tenkanen; Sinikka Uotila; Keith S. Wilson; Merja Penttilä; Kalevi Visuri

doi:10.1107/S0907444904019754

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

Sanna Askolin^*, Johan P. Turkenburg, Maija Tenkanen, Sinikka Uotila, Keith S. Wilson, Merja Penttilä, Kalevi Visuri

^*Corresponding author for this work

Not published at Aalto University

Research output: Contribution to journal › Article › Scientific › peer-review

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 Angstrom. The HFBI used in the crystallization experiments was purified from fungal cell walls.

Original language	English
Pages (from-to)	1903-1905
Number of pages	3
Journal	Acta Crystallographica. Section D: Biological Crystallography
Volume	60
DOIs	https://doi.org/10.1107/S0907444904019754
Publication status	Published - Oct 2004
MoE publication type	A1 Journal article-refereed

Keywords

PROTEINS

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10.1107/S0907444904019754

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

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 Angstrom. The HFBI used in the crystallization experiments was purified from fungal cell walls.",

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author = "Sanna Askolin and Turkenburg, \{Johan P.\} and Maija Tenkanen and Sinikka Uotila and Wilson, \{Keith S.\} and Merja Penttil{\"a} and Kalevi Visuri",

year = "2004",

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doi = "10.1107/S0907444904019754",

language = "English",

volume = "60",

pages = "1903--1905",

journal = "Acta Crystallographica. Section D: Biological Crystallography",

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TY - JOUR

T1 - Purification, crystallization and preliminary X-ray diffraction analysis of the Trichoderma reesei hydrophobin HFBI

AU - Askolin, Sanna

AU - Turkenburg, Johan P.

AU - Tenkanen, Maija

AU - Uotila, Sinikka

AU - Wilson, Keith S.

AU - Penttilä, Merja

AU - Visuri, Kalevi

PY - 2004/10

Y1 - 2004/10

N2 - 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 Angstrom. The HFBI used in the crystallization experiments was purified from fungal cell walls.

AB - 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 Angstrom. The HFBI used in the crystallization experiments was purified from fungal cell walls.

KW - PROTEINS

U2 - 10.1107/S0907444904019754

DO - 10.1107/S0907444904019754

M3 - Article

SN - 0907-4449

VL - 60

SP - 1903

EP - 1905

JO - Acta Crystallographica. Section D: Biological Crystallography

JF - Acta Crystallographica. Section D: Biological Crystallography

ER -

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

Abstract

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