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Crystallization and preliminary x-ray diffraction study of the flavoprotein NADH peroxidase from Streptococcus faecalis 10C1

MPG-Autoren
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Schiering,  Nikolaus
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Pai,  Emil F.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

https://www.sciencedirect.com/science/article/pii/S0021925819300584
(beliebiger Volltext)

https://www.jbc.org/article/S0021-9258(19)30058-4/fulltext
(beliebiger Volltext)

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Zitation

Schiering, N., Stoll, V. S., Blanchard, J. S.., & Pai, E. F. (1989). Crystallization and preliminary x-ray diffraction study of the flavoprotein NADH peroxidase from Streptococcus faecalis 10C1. The Journal of Biological Chemistry, 264(35), 21144-21145. Retrieved from https://pubmed.ncbi.nlm.nih.gov/2512289/.


Zitierlink: https://hdl.handle.net/21.11116/0000-000B-60DE-F
Zusammenfassung
NADH peroxidase from Streptococcus faecalis 10C1 has been crystallized from ammonium sulfate solutions using the hanging drop vapor diffusion method. Depending on pH, the crystals grew in the orthorhombic space group I222 or one of its subgroups P222 or P2(1)2(1)2 (or one of its two permutations). In both cases the unit cell axes are a = 76.6 A, b = 132.9 A, and c = 145.7 A. There are two monomers/asymmetric unit in the body-centered crystal form and four in the primitive one. The enzyme is catalytically active in the crystalline state. The crystals diffract to at least 2.5 A resolution; they are stable in the x-ray beam and hence suitable for detailed three-dimensional structure determination.