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Isolation, crystallization and preliminary X-ray diffraction data of human progastricsin
P K Ivanov1, M M Chernaya, A E Gustchina
1All-Union Cancer Research Centre, Moscow, USSR.
Biochimica Et Biophysica Acta
|September 3, 1990
Summary
Researchers crystallized human progastricsin, a precursor to gastric aspartic proteinases. These crystals are suitable for high-resolution X-ray analysis, advancing structural studies of these important enzymes.
Area of Science:
- Biochemistry
- Structural Biology
- Crystallography
Background:
- Human progastricsin is the zymogen form of gastric aspartic proteinases.
- Gastric aspartic proteinases play crucial roles in protein digestion.
Purpose of the Study:
- To isolate and crystallize human progastricsin for structural analysis.
- To determine the crystallographic properties of human progastricsin crystals.
Main Methods:
- Isolation and crystallization of human progastricsin.
- X-ray diffraction analysis of progastricsin crystals.
Main Results:
- Human progastricsin was successfully isolated and crystallized.
- The crystals belong to the tetragonal space group P4(2)2(1)2.
- Unit cell dimensions: a = b = 105.5 ± 0.1 Å, c = 70.6 Å.
- Native crystals diffract X-rays to at least 2.5 Å.
Conclusions:
- The obtained progastricsin crystals are suitable for high-resolution X-ray analysis.
- This facilitates detailed structural determination of human progastricsin.