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

N. Schiering, V. S. Stoll, John S. Blanchard, E. F. Pai

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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 P21212 (or one of its two permutations). In both cases the unit cell axes are a = 76.6 Å, b = 132.9 Å, and c = 145.7 Å. 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 Å resolution; they are stable in the x-ray beam and hence suitable for detailed three-dimensional structure determination.

Original languageEnglish (US)
Pages (from-to)21144-21145
Number of pages2
JournalJournal of Biological Chemistry
Volume264
Issue number35
StatePublished - 1989
Externally publishedYes

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NAD+ peroxidase
Flavoproteins
Enterococcus faecalis
Ammonium Sulfate
Crystallization
Diffraction
X-Rays
X rays
Crystals
Enzymes
Monomers
Vapors
Crystalline materials

ASJC Scopus subject areas

  • Biochemistry

Cite this

Crystallization and preliminary x-ray diffraction study of the flavoprotein NADH peroxidase from Streptococcus faecalis 10C1. / Schiering, N.; Stoll, V. S.; Blanchard, John S.; Pai, E. F.

In: Journal of Biological Chemistry, Vol. 264, No. 35, 1989, p. 21144-21145.

Research output: Contribution to journalArticle

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AU - Pai, E. F.

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