Crystallization and preliminary X-ray crystallographic analysis of a Trichoderma reesei β-mannanase from glycoside hydrolase family 5

Elisabetta Sabini, Andrzej M. Brzozowski, Miroslawa Dauter, Gideon J. Davies, Keith S. Wilson, Marja Paloheimo, Pirkko Suominen, Matti Siika-Aho, Merja Penttilä

Research output: Contribution to journalArticleScientificpeer-review

3 Citations (Scopus)

Abstract

Crystals of the catalytic core domain of a Trichoderma reesei β-mannanase belonging to glycoside hydrolase family 5 have been grown by the sitting-drop method at room temperature using ammonium sulfate as precipitant. The crystals grow as thin colourless plates and belong to space group P21, with unit-cell parameters a = 50.0, b = 54.3, c = 60.2 Å, β = 111.3°, and have a single monomer of mannanase in the asymmetric unit. Native data to 2.0 Å resolution have been collected at room temperature using synchrotron radiation. Data for a platinum derivative have been collected to 1.65 Å at 110 K in a very short time at the CCLRC Daresbury synchrotron source, using a charge-coupled device (CCD) as detector.

Original languageEnglish
Pages (from-to)1058-1060
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number5
DOIs
Publication statusPublished - 1 May 1999
MoE publication typeA1 Journal article-refereed

Fingerprint

glucosides
Synchrotrons
Trichoderma
Glycoside Hydrolases
Crystallization
Catalytic Domain
X-Rays
crystallization
X rays
Crystals
ammonium sulfates
Temperature
thin plates
Ammonium Sulfate
room temperature
Platinum
Synchrotron radiation
Charge coupled devices
crystals
charge coupled devices

Cite this

Sabini, Elisabetta ; Brzozowski, Andrzej M. ; Dauter, Miroslawa ; Davies, Gideon J. ; Wilson, Keith S. ; Paloheimo, Marja ; Suominen, Pirkko ; Siika-Aho, Matti ; Penttilä, Merja. / Crystallization and preliminary X-ray crystallographic analysis of a Trichoderma reesei β-mannanase from glycoside hydrolase family 5. In: Acta Crystallographica Section D: Biological Crystallography. 1999 ; Vol. 55, No. 5. pp. 1058-1060.
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abstract = "Crystals of the catalytic core domain of a Trichoderma reesei β-mannanase belonging to glycoside hydrolase family 5 have been grown by the sitting-drop method at room temperature using ammonium sulfate as precipitant. The crystals grow as thin colourless plates and belong to space group P21, with unit-cell parameters a = 50.0, b = 54.3, c = 60.2 {\AA}, β = 111.3°, and have a single monomer of mannanase in the asymmetric unit. Native data to 2.0 {\AA} resolution have been collected at room temperature using synchrotron radiation. Data for a platinum derivative have been collected to 1.65 {\AA} at 110 K in a very short time at the CCLRC Daresbury synchrotron source, using a charge-coupled device (CCD) as detector.",
author = "Elisabetta Sabini and Brzozowski, {Andrzej M.} and Miroslawa Dauter and Davies, {Gideon J.} and Wilson, {Keith S.} and Marja Paloheimo and Pirkko Suominen and Matti Siika-Aho and Merja Penttil{\"a}",
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Crystallization and preliminary X-ray crystallographic analysis of a Trichoderma reesei β-mannanase from glycoside hydrolase family 5. / Sabini, Elisabetta; Brzozowski, Andrzej M.; Dauter, Miroslawa; Davies, Gideon J.; Wilson, Keith S.; Paloheimo, Marja; Suominen, Pirkko; Siika-Aho, Matti; Penttilä, Merja.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 55, No. 5, 01.05.1999, p. 1058-1060.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Sabini, Elisabetta

AU - Brzozowski, Andrzej M.

AU - Dauter, Miroslawa

AU - Davies, Gideon J.

AU - Wilson, Keith S.

AU - Paloheimo, Marja

AU - Suominen, Pirkko

AU - Siika-Aho, Matti

AU - Penttilä, Merja

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