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Expression, purification, crystallization and preliminary characterization of an HHED aldolase homologue from Escherichia coli K12
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UNSPECIFIED (2002) Expression, purification, crystallization and preliminary characterization of an HHED aldolase homologue from Escherichia coli K12. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 58 (Part 12). pp. 2191-2193. doi:10.1107/S0907444902017894 ISSN 0907-4449.
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Official URL: http://dx.doi.org/10.1107/S0907444902017894
Abstract
An ORF designated b2245 (yfaU) in the Escherichia coli K12 genome sequence, identified as an HHED aldolase homologue, was cloned into the high-expression plasmid pT7-7 and overexpressed in E. coli B835(DE3). The enzyme was purified in three steps to 95% purity prior to crystallization. Crystals were obtained by the hanging-drop vapour-diffusion method at 277 K from a number of screening conditions. Crystals suitable for structural studies were grown from solutions containing 0.4 M ammonium dihydrogen phosphate and grew to a maximum dimension of approximately 0.5 mm. Diffraction data to 1.7 Angstrom were collected using an in-house Cu Kalpha radiation source at 100 K. The crystals belong to space group C222(1), with unit-cell parameters a = 105.1, b = 136.6, c = 123.1 Angstrom. A 90% complete data set was collected to 1.78 Angstrom from a single native crystal using in-house facilities.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
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Journal or Publication Title: | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | ||||
Publisher: | BLACKWELL MUNKSGAARD | ||||
ISSN: | 0907-4449 | ||||
Official Date: | December 2002 | ||||
Dates: |
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Volume: | 58 | ||||
Number: | Part 12 | ||||
Number of Pages: | 3 | ||||
Page Range: | pp. 2191-2193 | ||||
DOI: | 10.1107/S0907444902017894 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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