Expression, purification and preliminary X-ray diffraction studies of RebC
| Autor: | Katherine Groom, Anupam Bhattacharya, Zongchao Jia, Laura M. van Staalduinen, David L. Zechel |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Rebeccamycin
Biophysics Indolocarbazole medicine.disease_cause Crystallography X-Ray Biochemistry Mixed Function Oxygenases chemistry.chemical_compound Structural Biology Actinomycetales Genetics medicine Escherichia coli Cloning Molecular chemistry.chemical_classification biology Space group food and beverages Monooxygenase Condensed Matter Physics biology.organism_classification Crystallography enzymes and coenzymes (carbohydrates) Enzyme chemistry Crystallization Communications X-ray crystallography biological sciences health occupations bacteria Crystallization medicine.drug |
| Zdroj: | Acta crystallographica. Section F, Structural biology and crystallization communications. 63(Pt 11) |
| ISSN: | 1744-3091 |
| Popis: | The flavin-dependent monooxygenase RebC is a key enzyme in the biosynthesis of the indolocarbazole rebeccamycin. The synthesis of rebeccamycin is of great interest as it has been shown to be a natural antitumour agent. The enzyme has been recombinantly expressed in Escherichia coli and purified to homogeneity. Hanging-drop vapour diffusion in combination with microseeding was used to obtain suitable crystals for X-ray diffraction. Data were collected to 2.4 A; the crystals belonged to space group P2(1), with unit-cell parameters a = 63.08, b = 77.85, c = 63.94 A, alpha = gamma = 90, beta = 108.11 degrees . |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text