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Crystallization and preliminary X-ray analysis of human angiogenin
K R Acharya1, V Subramanian, R Shapiro
1Department of Biochemistry, University of Bath, Claverton Down, U.K.
Journal of Molecular Biology
|December 20, 1992
Summary
Recombinant human angiogenin crystals were successfully grown using sodium potassium tartrate and polyethylene glycol. These crystals are suitable for detailed three-dimensional X-ray structural analysis.
Area of Science:
- Protein crystallography
- Structural biology
- Biochemistry
Background:
- Recombinant human angiogenin is a protein with significant biological roles.
- Understanding its structure is crucial for functional studies.
Purpose of the Study:
- To obtain high-quality crystals of recombinant human angiogenin.
- To determine the crystallographic parameters for structural analysis.
Main Methods:
- Crystallization of recombinant human angiogenin.
- Use of sodium potassium tartrate and polyethylene glycol as precipitants.
- X-ray diffraction analysis.
Main Results:
- Crystals of recombinant human angiogenin were successfully grown.
- The crystals belong to space group C222(1) with specific unit cell dimensions.
- The crystals diffract X-rays to a resolution of at least 2.3 A.
Conclusions:
- The grown crystals are well-ordered and suitable for X-ray structural determination.
- This facilitates detailed three-dimensional structural analysis of recombinant human angiogenin.