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Published on: January 16, 2014
Preliminary X-ray crystallographic analysis of a modified basic fibroblast growth factor
D M Bollag1, A P Seddon, P Böhlen
1Department of Chemistry, Princeton University, NJ 08544.
Journal of Molecular Biology
|April 5, 1991
Summary
Modified human basic fibroblast growth factor (hbFGF) was successfully crystallized. These protein crystals are triclinic and diffract X-rays to 2 angstroms, enabling structural analysis.
Area of Science:
- Biochemistry and structural biology
- Protein engineering and crystallography
Background:
- Human basic fibroblast growth factor (hbFGF) is crucial for cell growth and tissue repair.
- Understanding hbFGF structure is key to developing targeted therapies.
Purpose of the Study:
- To engineer and crystallize a modified form of hbFGF for structural determination.
- To characterize the crystal properties of the engineered hbFGF.
Main Methods:
- Site-directed mutagenesis was used to substitute Ala3 and Ser5 with glutamic acid in hbFGF.
- Purification of the recombinant protein.
- X-ray diffraction analysis of the resulting crystals.
Main Results:
- The engineered hbFGF protein was successfully purified.
- Triclinic crystals of the modified hbFGF were obtained.
- The crystals belong to space group P1 with unit cell parameters a = 31.0 A, b = 33.6 A, c = 34.7 A, alpha = 88°, beta = 85°, gamma = 76°.
- The crystals diffract X-rays to a resolution of at least 2 A.
Conclusions:
- The modified hbFGF protein can be crystallized.
- The obtained crystals are suitable for high-resolution structural studies.
- This work provides a foundation for determining the three-dimensional structure of hbFGF.
