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Crystallographic studies on D-amino acid oxidase
The Journal of Biological Chemistry
|October 25, 1978
Summary
Hog kidney D-amino acid oxidase (DAO) was crystallized into two distinct forms: orthorhombic prisms at pH 8.3 and trigonal prisms at lower pH. Both crystal structures reveal highly associated protein structures.
Area of Science:
- Biochemistry
- Crystallography
- Enzymology
Background:
- D-amino acid oxidase (DAO) is a flavoprotein enzyme found in hog kidneys.
- Understanding the structural properties of DAO is crucial for its functional characterization.
Purpose of the Study:
- To crystallize D-amino acid oxidase (DAO) from hog kidneys.
- To determine the structural characteristics of different DAO crystal forms.
Main Methods:
- Enzyme crystallization using the enzyme-benzoate complex.
- X-ray crystallography to determine crystal space groups and cell dimensions.
Main Results:
- Two distinct crystal forms of DAO were obtained: orthorhombic prisms (space group C2221) at pH 8.3 and trigonal prisms (space group P3112 or enantiomorph) at lower pH.
- Specific unit cell dimensions were determined for each crystal form.
- Crystallization was successful at 28°C, with limited success at 4°C.
- Both crystalline forms exhibited highly associated protein structures.
Conclusions:
- D-amino acid oxidase (DAO) can be crystallized in multiple forms, providing opportunities for detailed structural analysis.
- The observed protein association in crystalline states may offer insights into DAO's quaternary structure and function.