Abstract
Soybean lipoxygenase-3 has been crystallized by the vapor diffusion method in 16-20% polyethylene glycol (average M(r), 3,400), 0.2 M sodium acetate buffer, pH 5.7, at 21 degrees C, at a protein concentration of 8-15 mg/mL. The crystals, which diffract to 3-A spacings, belong to the monoclinic space group C2. Cell constants are a = 111.9, b = 136.4, and c = 61.6 A and beta = 95.7 degrees. The calculated value of Matthews's constant, Vm = 2.48 A3/kDa, is consistent with the presence of one molecule of lipoxygenase per crystallographic asymmetric unit (Z = 4).
Full Text
The Full Text of this article is available as a PDF (2.0 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Boyington J. C., Gaffney B. J., Amzel L. M. The three-dimensional structure of an arachidonic acid 15-lipoxygenase. Science. 1993 Jun 4;260(5113):1482–1486. doi: 10.1126/science.8502991. [DOI] [PubMed] [Google Scholar]
- Christopher J. P., Pistorius E. K., Regnier F. E., Axelrod B. Factors influencing the positional specificity of soybean lipoxygenase. Biochim Biophys Acta. 1972 Nov 10;289(1):82–87. doi: 10.1016/0005-2744(72)90110-6. [DOI] [PubMed] [Google Scholar]
- Ford-Hutchinson A. W., Gresser M., Young R. N. 5-Lipoxygenase. Annu Rev Biochem. 1994;63:383–417. doi: 10.1146/annurev.bi.63.070194.002123. [DOI] [PubMed] [Google Scholar]
- Gardner H. W. Recent investigations into the lipoxygenase pathway of plants. Biochim Biophys Acta. 1991 Jul 30;1084(3):221–239. doi: 10.1016/0005-2760(91)90063-n. [DOI] [PubMed] [Google Scholar]
- Matthews B. W. Solvent content of protein crystals. J Mol Biol. 1968 Apr 28;33(2):491–497. doi: 10.1016/0022-2836(68)90205-2. [DOI] [PubMed] [Google Scholar]
- Minor W., Steczko J., Bolin J. T., Otwinowski Z., Axelrod B. Crystallographic determination of the active site iron and its ligands in soybean lipoxygenase L-1. Biochemistry. 1993 Jun 29;32(25):6320–6323. doi: 10.1021/bi00076a003. [DOI] [PubMed] [Google Scholar]
- Shibata D., Steczko J., Dixon J. E., Andrews P. C., Hermodson M., Axelrod B. Primary structure of soybean lipoxygenase L-2. J Biol Chem. 1988 May 15;263(14):6816–6821. [PubMed] [Google Scholar]
- Steczko J., Axelrod B. Identification of the iron-binding histidine residues in soybean lipoxygenase L-1. Biochem Biophys Res Commun. 1992 Jul 31;186(2):686–689. doi: 10.1016/0006-291x(92)90801-q. [DOI] [PubMed] [Google Scholar]
- Steczko J., Donoho G. P., Clemens J. C., Dixon J. E., Axelrod B. Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement. Biochemistry. 1992 Apr 28;31(16):4053–4057. doi: 10.1021/bi00131a022. [DOI] [PubMed] [Google Scholar]
- Steczko J., Muchmore C. R., Smith J. L., Axelrod B. Crystallization and preliminary X-ray investigation of lipoxygenase 1 from soybeans. J Biol Chem. 1990 Jul 5;265(19):11352–11354. [PubMed] [Google Scholar]
- Yamamoto S. Mammalian lipoxygenases: molecular structures and functions. Biochim Biophys Acta. 1992 Oct 30;1128(2-3):117–131. doi: 10.1016/0005-2760(92)90297-9. [DOI] [PubMed] [Google Scholar]