Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei

Christina Divne, Irmgard Sinning, Jerry Ståhlberg, Göran Pettersson, Michael Bailey, Matti Siika-aho, Emilio Margolles-Clark, Tuula Teeri, Alwyn Jones

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

The catalytic core domains of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from Trichoderma reesei have been crystallized using the hanging drop vapour diffusion method. In the case of CBHI, use of polyethylene glycol 20,000, and calcium chloride at low pH produced good quality single crystals suitable for X-ray studies. The crystals belong to a primitive orthorhombic space group with unit cell dimensions a = 84·0 Å, b = 86·2 Å, c = 111·8 Å, and diffract beyond 2·0 Å resolution. Bipyramidal crystals of EGI core were grown from ammonium sulphate at pH 7·5. The crystals are tetragonal, either P 4122 or the enantiomorph P4322, with cell dimensions a = b = 101·8 Å and c = 198·0 Å, and at best diffract to a resolution of 2·5 Å.

Original languageEnglish
Pages (from-to)905 - 907
Number of pages3
JournalJournal of Molecular Biology
Volume234
Issue number3
DOIs
Publication statusPublished - 1993
MoE publication typeA1 Journal article-refereed

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Cellulose 1,4-beta-Cellobiosidase
Cellulases
Trichoderma
Crystallization
Catalytic Domain
X-Rays
Calcium Chloride
Ammonium Sulfate
Proteins

Cite this

Divne, Christina ; Sinning, Irmgard ; Ståhlberg, Jerry ; Pettersson, Göran ; Bailey, Michael ; Siika-aho, Matti ; Margolles-Clark, Emilio ; Teeri, Tuula ; Jones, Alwyn. / Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei. In: Journal of Molecular Biology. 1993 ; Vol. 234, No. 3. pp. 905 - 907.
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title = "Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei",
abstract = "The catalytic core domains of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from Trichoderma reesei have been crystallized using the hanging drop vapour diffusion method. In the case of CBHI, use of polyethylene glycol 20,000, and calcium chloride at low pH produced good quality single crystals suitable for X-ray studies. The crystals belong to a primitive orthorhombic space group with unit cell dimensions a = 84·0 {\AA}, b = 86·2 {\AA}, c = 111·8 {\AA}, and diffract beyond 2·0 {\AA} resolution. Bipyramidal crystals of EGI core were grown from ammonium sulphate at pH 7·5. The crystals are tetragonal, either P 4122 or the enantiomorph P4322, with cell dimensions a = b = 101·8 {\AA} and c = 198·0 {\AA}, and at best diffract to a resolution of 2·5 {\AA}.",
author = "Christina Divne and Irmgard Sinning and Jerry St{\aa}hlberg and G{\"o}ran Pettersson and Michael Bailey and Matti Siika-aho and Emilio Margolles-Clark and Tuula Teeri and Alwyn Jones",
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Divne, C, Sinning, I, Ståhlberg, J, Pettersson, G, Bailey, M, Siika-aho, M, Margolles-Clark, E, Teeri, T & Jones, A 1993, 'Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei', Journal of Molecular Biology, vol. 234, no. 3, pp. 905 - 907. https://doi.org/10.1006/jmbi.1993.1640

Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei. / Divne, Christina; Sinning, Irmgard; Ståhlberg, Jerry; Pettersson, Göran; Bailey, Michael; Siika-aho, Matti; Margolles-Clark, Emilio; Teeri, Tuula; Jones, Alwyn.

In: Journal of Molecular Biology, Vol. 234, No. 3, 1993, p. 905 - 907.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Crystallization and preliminary X-ray studies on the core proteins of cellobiohydrolase I and endoglucanase I from Trichoderma reesei

AU - Divne, Christina

AU - Sinning, Irmgard

AU - Ståhlberg, Jerry

AU - Pettersson, Göran

AU - Bailey, Michael

AU - Siika-aho, Matti

AU - Margolles-Clark, Emilio

AU - Teeri, Tuula

AU - Jones, Alwyn

N1 - Project code: BIO1004

PY - 1993

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N2 - The catalytic core domains of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from Trichoderma reesei have been crystallized using the hanging drop vapour diffusion method. In the case of CBHI, use of polyethylene glycol 20,000, and calcium chloride at low pH produced good quality single crystals suitable for X-ray studies. The crystals belong to a primitive orthorhombic space group with unit cell dimensions a = 84·0 Å, b = 86·2 Å, c = 111·8 Å, and diffract beyond 2·0 Å resolution. Bipyramidal crystals of EGI core were grown from ammonium sulphate at pH 7·5. The crystals are tetragonal, either P 4122 or the enantiomorph P4322, with cell dimensions a = b = 101·8 Å and c = 198·0 Å, and at best diffract to a resolution of 2·5 Å.

AB - The catalytic core domains of cellobiohydrolase I (CBHI) and endoglucanase I (EGI) from Trichoderma reesei have been crystallized using the hanging drop vapour diffusion method. In the case of CBHI, use of polyethylene glycol 20,000, and calcium chloride at low pH produced good quality single crystals suitable for X-ray studies. The crystals belong to a primitive orthorhombic space group with unit cell dimensions a = 84·0 Å, b = 86·2 Å, c = 111·8 Å, and diffract beyond 2·0 Å resolution. Bipyramidal crystals of EGI core were grown from ammonium sulphate at pH 7·5. The crystals are tetragonal, either P 4122 or the enantiomorph P4322, with cell dimensions a = b = 101·8 Å and c = 198·0 Å, and at best diffract to a resolution of 2·5 Å.

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