Crystallization and preliminary X-ray characterization of Trichoderma reesei hydrophobin HFBII

Johanna Hakanpää, Tarja Parkkinen, Nina Hakulinen, Markus Linder, Juha Rouvinen

Research output: Contribution to journalArticleScientificpeer-review

20 Citations (Scopus)

Abstract

Hydrophobins are small proteins found in filamentous fungi and characterized by their ability to change the character of a surface by spontaneous self-assembly on a hydrophobic-hydrophilic interface. Hydrophobin HFBII from Trichoderma reesei was crystallized by the hanging-drop vapour-diffusion method at 293 K. Two crystal forms were obtained: a native form and a form crystallized in the presence of manganese chloride. The native crystals were of high symmetry, cubic I23, but only diffracted to 3.25 Å. The crystals grown in the presence of manganese were monoclinic and diffracted to 1.0 Å with a synchrotron-radiation source. The anomalous difference Patterson map calculated from the home laboratory data showed a strong single peak, possibly caused by manganese present in the crystallization solution.
Original languageEnglish
Pages (from-to)163 - 165
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number1
DOIs
Publication statusPublished - 2004
MoE publication typeA1 Journal article-refereed

Fingerprint

Trichoderma
Manganese
Crystallization
X-Rays
Synchrotrons
Fungi
Radiation
Proteins
manganese chloride

Keywords

  • proteins
  • hydrophobins
  • filamentous fungi
  • Trichoderma reesei
  • crystallization

Cite this

Hakanpää, Johanna ; Parkkinen, Tarja ; Hakulinen, Nina ; Linder, Markus ; Rouvinen, Juha. / Crystallization and preliminary X-ray characterization of Trichoderma reesei hydrophobin HFBII. In: Acta Crystallographica Section D: Biological Crystallography. 2004 ; Vol. 60, No. 1. pp. 163 - 165.
@article{2ec0e93b1acf45cd9ff88fe8316fb507,
title = "Crystallization and preliminary X-ray characterization of Trichoderma reesei hydrophobin HFBII",
abstract = "Hydrophobins are small proteins found in filamentous fungi and characterized by their ability to change the character of a surface by spontaneous self-assembly on a hydrophobic-hydrophilic interface. Hydrophobin HFBII from Trichoderma reesei was crystallized by the hanging-drop vapour-diffusion method at 293 K. Two crystal forms were obtained: a native form and a form crystallized in the presence of manganese chloride. The native crystals were of high symmetry, cubic I23, but only diffracted to 3.25 {\AA}. The crystals grown in the presence of manganese were monoclinic and diffracted to 1.0 {\AA} with a synchrotron-radiation source. The anomalous difference Patterson map calculated from the home laboratory data showed a strong single peak, possibly caused by manganese present in the crystallization solution.",
keywords = "proteins, hydrophobins, filamentous fungi, Trichoderma reesei, crystallization",
author = "Johanna Hakanp{\"a}{\"a} and Tarja Parkkinen and Nina Hakulinen and Markus Linder and Juha Rouvinen",
year = "2004",
doi = "10.1107/S0907444903024430",
language = "English",
volume = "60",
pages = "163 -- 165",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "2059-7983",
publisher = "Wiley",
number = "1",

}

Crystallization and preliminary X-ray characterization of Trichoderma reesei hydrophobin HFBII. / Hakanpää, Johanna; Parkkinen, Tarja; Hakulinen, Nina; Linder, Markus; Rouvinen, Juha.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 60, No. 1, 2004, p. 163 - 165.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Crystallization and preliminary X-ray characterization of Trichoderma reesei hydrophobin HFBII

AU - Hakanpää, Johanna

AU - Parkkinen, Tarja

AU - Hakulinen, Nina

AU - Linder, Markus

AU - Rouvinen, Juha

PY - 2004

Y1 - 2004

N2 - Hydrophobins are small proteins found in filamentous fungi and characterized by their ability to change the character of a surface by spontaneous self-assembly on a hydrophobic-hydrophilic interface. Hydrophobin HFBII from Trichoderma reesei was crystallized by the hanging-drop vapour-diffusion method at 293 K. Two crystal forms were obtained: a native form and a form crystallized in the presence of manganese chloride. The native crystals were of high symmetry, cubic I23, but only diffracted to 3.25 Å. The crystals grown in the presence of manganese were monoclinic and diffracted to 1.0 Å with a synchrotron-radiation source. The anomalous difference Patterson map calculated from the home laboratory data showed a strong single peak, possibly caused by manganese present in the crystallization solution.

AB - Hydrophobins are small proteins found in filamentous fungi and characterized by their ability to change the character of a surface by spontaneous self-assembly on a hydrophobic-hydrophilic interface. Hydrophobin HFBII from Trichoderma reesei was crystallized by the hanging-drop vapour-diffusion method at 293 K. Two crystal forms were obtained: a native form and a form crystallized in the presence of manganese chloride. The native crystals were of high symmetry, cubic I23, but only diffracted to 3.25 Å. The crystals grown in the presence of manganese were monoclinic and diffracted to 1.0 Å with a synchrotron-radiation source. The anomalous difference Patterson map calculated from the home laboratory data showed a strong single peak, possibly caused by manganese present in the crystallization solution.

KW - proteins

KW - hydrophobins

KW - filamentous fungi

KW - Trichoderma reesei

KW - crystallization

U2 - 10.1107/S0907444903024430

DO - 10.1107/S0907444903024430

M3 - Article

VL - 60

SP - 163

EP - 165

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 2059-7983

IS - 1

ER -