Crystallization of recombinant chitobiase from Serratia marcescens
Crystallization of recombinant chitobiase from Serratia marcescens
We are currently investigating the biochemical and structural properties of both chitin degrading enzymes chitinase and chitobiase from Serratia marcescens. Previously we have reported the first crystallization and characterization of chitinase crystals (Vorgias et al., 1992). In this communication we present the first crystallization of chitobiase. The protein was synthesized in Escherichia coli and purified to homogeneity using cation exchange chromatography and fast protein liquid chromatography. The crystals have the shape of small prisms and the space group is P21 with β = 101.0 ° and unit cell dimensions a = 63.2 A ̊, b = 133.2 A ̊, c = 55.1 A ̊. They diffract X-rays to about 2.5 Å resolution and are suitable for three-dimensional structural analysis.
696-697
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Dauter, Zbigniew
18859865-99e0-40d6-bf0b-9636d21a0146
Oppenheim, Amos B.
3512b7e9-e3d7-4e7c-b61a-6efdea6bc84c
Vorgias, Constantin E.
cf1c21bf-bc10-44ab-ba08-9d2baf07dda1
20 November 1992
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Dauter, Zbigniew
18859865-99e0-40d6-bf0b-9636d21a0146
Oppenheim, Amos B.
3512b7e9-e3d7-4e7c-b61a-6efdea6bc84c
Vorgias, Constantin E.
cf1c21bf-bc10-44ab-ba08-9d2baf07dda1
Tews, Ivo, Dauter, Zbigniew, Oppenheim, Amos B. and Vorgias, Constantin E.
(1992)
Crystallization of recombinant chitobiase from Serratia marcescens.
Journal of Molecular Biology, 228 (2), .
(doi:10.1016/0022-2836(92)90853-C).
Abstract
We are currently investigating the biochemical and structural properties of both chitin degrading enzymes chitinase and chitobiase from Serratia marcescens. Previously we have reported the first crystallization and characterization of chitinase crystals (Vorgias et al., 1992). In this communication we present the first crystallization of chitobiase. The protein was synthesized in Escherichia coli and purified to homogeneity using cation exchange chromatography and fast protein liquid chromatography. The crystals have the shape of small prisms and the space group is P21 with β = 101.0 ° and unit cell dimensions a = 63.2 A ̊, b = 133.2 A ̊, c = 55.1 A ̊. They diffract X-rays to about 2.5 Å resolution and are suitable for three-dimensional structural analysis.
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Published date: 20 November 1992
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Local EPrints ID: 500818
URI: http://eprints.soton.ac.uk/id/eprint/500818
ISSN: 0022-2836
PURE UUID: 06b3324c-4350-4081-a039-ac62a7c96684
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Date deposited: 13 May 2025 17:18
Last modified: 14 May 2025 01:44
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Author:
Zbigniew Dauter
Author:
Amos B. Oppenheim
Author:
Constantin E. Vorgias
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