The recombinant homodimeric hemoglobin from the strictly aerobe gram-negative bacterium Vitreoscilla stercoraria has been expressed in Escherichia coli, purified to homogeneity, and crystallized by vapor diffusion techniques, using ammonium sulfate as precipitant. The crystals belong to the monoclin
Crystallization and preliminary x-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium Simplicissimum
โ Scribed by Andrea Mattevi; Marco W. Fraaije; Alessandro Coda; Willem J.H. van Berkel
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 37 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0887-3585
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โฆ Synopsis
Vanillyl-alcohol oxidase catalyses the oxidation of several 4-hydroxybenzyl alcohols by using 8-alpha-(N3-histidyl)-FAD as a covalently bound prosthetic group. Crystals of vanillyl-alcohol oxidase from Penicillium simplicissimum have been grown by using the vapor diffusion technique. The space group was found to be I, with cell dimensions a = b = 140.5 A, c = 132.9 A. Diffraction data have been recorded to 3.2 A resolution by using a laboratory source and to 2.5 A resolution on flash freezing the crystal at the ELETTRA Synchrotron X-ray diffraction beam line.
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