Chicken liver basic fatty acid-binding protein (pI = 9.0). Purification, crystallization and preliminary X-ray data

Area of Science:

• Biochemistry
• Structural Biology
• Crystallography

Background:

• Basic fatty acid-binding proteins (B-FABPs) are crucial for lipid metabolism.
• Understanding the structure of B-FABPs provides insights into their function and interactions.

Purpose of the Study:

• To purify chicken liver B-FABP.
• To obtain high-quality crystals of chicken liver B-FABP suitable for X-ray diffraction analysis.

Main Methods:

• Purification of chicken liver B-FABP using a modified rat liver purification protocol.
• Crystallization of the purified protein.
• X-ray diffraction analysis of the obtained crystals.

Main Results:

• High-yield purification of homogeneous chicken liver B-FABP achieved.
• Two distinct crystal forms were obtained: tetragonal (P4(2)2(1)2) and orthorhombic (P2(1)2(1)2(1)).
• The orthorhombic crystals diffracted to at least 2.8 A resolution and are suitable for structural studies.

Conclusions:

• Chicken liver B-FABP can be readily purified and crystallized.
• The orthorhombic crystal form is promising for determining the protein's three-dimensional structure.
• This structural information will aid in understanding B-FABP function in lipid transport and metabolism.