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Atomic resolution structure of concanavalin A at 120 K
1Biology and Biotechnology Research Program, Lawrence Livermore National Laboratory, CA 94550, USA. sp@oedipus.llnl.gov
Acta Crystallographica. Section D, Biological Crystallography
|November 1, 1996
Summary
This study presents a high-resolution 1.2 A structure of native concanavalin A, revealing detailed atomic arrangements and water molecule interactions. The refined protein structure provides insights into concanavalin A
Area of Science:
- Biochemistry
- Structural Biology
- Crystallography
Background:
- Concanavalin A is a legume lectin with known biological functions.
- High-resolution structural data is crucial for understanding protein-ligand interactions and enzymatic mechanisms.
Purpose of the Study:
- To refine the three-dimensional structure of native concanavalin A at near-atomic resolution.
- To provide an updated structural model for further functional and mechanistic studies.
Main Methods:
- X-ray diffraction data collection at 120 K.
- Crystallographic refinement using SHELXL software.
- Analysis of protein, metal ion, and water molecule positions.
Main Results:
- A high-resolution (1.2 A) structure of native concanavalin A was determined.
- The crystal structure revealed 237 amino acids, two metal ions, and 271 water molecules.
- Disorder in 30 amino-acid side chains was modeled across two conformations.
Conclusions:
- The refined structure offers an unprecedented level of detail for native concanavalin A.
- This structural model serves as a foundation for investigating concanavalin A's biological roles and interactions.