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Human plasminogen kringle 4. Crystallization and preliminary diffraction data of two different crystal forms.
A M Mulichak1, C H Park, A Tulinsky
1Department of Chemistry, Michigan State University, East Lansing 48824.
The Journal of Biological Chemistry
|February 5, 1989
Summary
Human plasminogen kringle 4 was crystallized in two forms, yielding high-resolution X-ray diffraction data. This structural information is crucial for understanding plasminogen function and related biological processes.
Area of Science:
- Biochemistry
- Structural Biology
- Crystallography
Background:
- Plasminogen kringle 4 is a key domain involved in fibrinolysis.
- Understanding its structure is essential for elucidating its biological functions.
Purpose of the Study:
- To determine the crystal structure of human plasminogen kringle 4.
- To obtain high-resolution data for structural analysis.
Main Methods:
- Crystallization of human plasminogen kringle 4 in monoclinic and orthorhombic forms.
- X-ray diffraction analysis to 2.0 A resolution.
- Calculation of self-rotation function for monoclinic data.
Main Results:
- Two distinct crystal forms (monoclinic and orthorhombic) were obtained.
- Both crystal forms diffracted X-rays to 2.0 A resolution.
- A non-crystallographic 2-fold rotation was identified in the monoclinic crystal form.
Conclusions:
- The successful crystallization and diffraction of human plasminogen kringle 4 provide a basis for detailed structural studies.
- Further analysis, including cross-rotation functions, will aid in solving the structure.
- This research contributes to the understanding of plasminogen structure-function relationships.