Crystallization and X-ray diffraction analysis of 6-aminohexanoate-dimer hydrolase from Arthrobacter sp. KI72
| Autor: | Naoki Shibata, Taku Ohki, Nobuhiro Mizuno, Yoshiki Higuchi, Masahiro Takeo, Seiji Negoro |
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| Rok vydání: | 2005 |
| Předmět: |
Protein Conformation
Biophysics Crystallography X-Ray Biochemistry law.invention Amidohydrolases Crystal Diffusion chemistry.chemical_compound Structure-Activity Relationship X-Ray Diffraction Structural Biology law Arthrobacter Sodium citrate Hydrolase Genetics Escherichia coli Imidazole Crystallization biology Space group Hydrogen-Ion Concentration Condensed Matter Physics biology.organism_classification Protein Structure Tertiary Crystallography Nylons Biodegradation Environmental chemistry Ammonium Sulfate Crystallization Communications X-ray crystallography biological sciences bacteria Electrophoresis Polyacrylamide Gel Dimerization Plasmids |
| Zdroj: | Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 10) |
| ISSN: | 1744-3091 |
| Popis: | To investigate the structure-function relationship between 6-aminohexanoate-dimer hydrolase (EII) from Arthrobacter sp. and a cryptic protein (EII') which shows 88% sequence identity to EII, a hybrid protein (named Hyb-24) of EII and EII' was overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method with ammonium sulfate as a precipitant in MES buffer pH 6.5. The crystal belongs to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 96.37, c = 113.09 A. Diffraction data were collected from native and methylmercuric chloride derivative crystals to resolutions of 1.75 and 1.80 A, respectively. |
| Databáze: | OpenAIRE |
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