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The Journal of biological chemistry1990; 265(25); 14886-14887;

Crystallization of a calcium-binding lysozyme from horse milk.

Abstract: Crystals of the calcium-containing lysozyme from horse milk have been grown by precipitation with sodium phosphate. The crystals are orthorhombic space group P2(1)2(1)2(1) with cell dimensions a = 53.2, b = 57.1, and c = 38.2 A and contain a single molecule in the asymmetric unit. The crystals are suitable for high resolution x-ray structural analysis.
Publication Date: 1990-09-05 PubMed ID: 2394704
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  • Comparative Study
  • Journal Article
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research article is about successfully growing calcium-binding protein crystals extracted from horse milk using sodium phosphate. These crystals, according to the scientists, could potentially be used in high resolution x-ray structural analysis.

Process of Crystallization

  • The researchers in this study managed to crystallize a certain calcium-binding lysozyme (protein) obtained from horse milk.
  • The process of crystallization was carried out by precipitation with sodium phosphate. Precipitation is a common technique used in chemistry to form solid particles within a solution.

Nature of the Crystals

  • The crystals formed belonged to the orthorhombic space group P2(1)2(1)2(1). The orthorhombic system is one of the seven crystal systems used to describe the shapes of crystals. It consists of three unequal axes all intersecting at 90 degrees.
  • The dimensions of the crystalline structure are 53.2, 57.1, and 38.2 Angstroms (a unit of measurement used in crystallography).
  • Each crystal contains a single molecule within the asymmetric unit. An asymmetric unit, in crystallographic terms, refers to the smallest part of the crystal lattice that, when repeated, can generate the entire crystal structure.

Potential Applications

  • The crystals were deemed suitable for high-resolution x-ray structural analysis. This is a technique used to determine the atomic and molecular structure of a crystal. With this technique, scientists can pinpoint where each atom is located in the crystal and how it interacts with the surrounding atoms.

Cite This Article

APA
Zeng J, Rao KR, Brew K, Fenna R. (1990). Crystallization of a calcium-binding lysozyme from horse milk. J Biol Chem, 265(25), 14886-14887.

Publication

ISSN: 0021-9258
NlmUniqueID: 2985121R
Country: United States
Language: English
Volume: 265
Issue: 25
Pages: 14886-14887

Researcher Affiliations

Zeng, J
  • Department of Biochemistry and Molecular Biology, University of Miami Medical School, Florida 33101.
Rao, K R
    Brew, K
      Fenna, R

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Binding Sites
        • Calcium / metabolism
        • Crystallization
        • Female
        • Horses
        • Humans
        • Milk / enzymology
        • Milk, Human / enzymology
        • Molecular Sequence Data
        • Muramidase / genetics
        • Muramidase / isolation & purification
        • Muramidase / metabolism
        • Pregnancy
        • Sequence Homology, Nucleic Acid
        • X-Ray Diffraction

        Grant Funding

        • GM21363 / NIGMS NIH HHS

        Citations

        This article has been cited 1 times.
        1. Acharya KR, Stuart DI, Phillips DC, McKenzie HA, Teahan CG. Models of the three-dimensional structures of echidna, horse, and pigeon lysozymes: calcium-binding lysozymes and their relationship with alpha-lactalbumins. J Protein Chem 1994 Aug;13(6):569-84.
          doi: 10.1007/BF01901539pubmed: 7832986google scholar: lookup