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Crystallization and preliminary crystallographic data for bovine antithrombin III.
J P Samama1, M Delarue, L Mourey
1Laboratoire de Cristallographie Biologique, I.B.M.C. du C.N.R.S., Strasbourg, France.
Journal of Molecular Biology
|December 20, 1989
Summary
Bovine antithrombin III crystals were successfully obtained, revealing structural details. Analysis indicates protein molecules are cleaved at the active site, offering insights into antithrombin structure and function.
Area of Science:
- Biochemistry
- Structural Biology
- Crystallography
Background:
- Antithrombin III is a crucial proteinase inhibitor in blood plasma.
- Understanding its structure is key to comprehending its inhibitory mechanisms.
Purpose of the Study:
- To crystallize bovine antithrombin III and determine its crystal structure.
- To investigate potential modifications or cleavage of the protein within the crystals.
Main Methods:
- Crystallization of bovine antithrombin III using metal ions and ammonium sulfate.
- X-ray diffraction analysis to determine space group and cell parameters.
- Electrophoresis and N-terminal amino acid sequencing of redissolved crystals.
Main Results:
- Crystals of bovine antithrombin III were obtained, belonging to space group P4(1)2(1)2 or P4(3)2(1)2.
- Unit cell dimensions were determined as a = b = 91.4 A, c = 383.1 A.
- Evidence suggests protein molecules are cleaved at the active site.
Conclusions:
- The study provides crystallographic data for bovine antithrombin III.
- The observed cleavage indicates potential post-translational modification or degradation within the crystal environment.