Crystallization and preliminary diffraction data for horse heart metmyoglobin

Area of Science:

• Biochemistry
• Structural Biology
• Crystallography

Background:

• Metmyoglobin is a form of myoglobin where the iron in the heme group is oxidized.
• Understanding the structure of metmyoglobin is crucial for elucidating its function and interactions.

Purpose of the Study:

• To obtain well-ordered crystals of horse heart metmyoglobin suitable for X-ray diffraction analysis.
• To investigate the crystallization behavior of horse heart myoglobin derivatives with modified heme prosthetic groups.

Main Methods:

• Crystallization of metmyoglobin using hanging drop and batch methods.
• X-ray diffraction analysis of obtained crystals.
• Preparation and crystallization of myoglobin derivatives with altered heme groups.

Main Results:

• Reddish-brown crystals of horse heart metmyoglobin were successfully obtained in space group P2(1).
• Crystallographic data: a = 64.3 A, b = 28.9 A, c = 35.9 A, beta = 107.1 degrees.
• Morphologically similar crystal forms were achieved for three horse heart myoglobin derivatives with modified heme groups.

Conclusions:

• The crystallization methods employed are effective for obtaining horse heart metmyoglobin crystals.
• The structural integrity of myoglobin is maintained in its metmyoglobin form and with modified heme groups, allowing for structural studies.