Crystallization, preliminary X-ray analysis and molecular-replacement solution of the carboxy form of haemoglobin I from the fish Brycon cephalus

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 56; no. 12; pp. 1685 - 1687
• Main Authors: Honda, R. T., Delatorre, P., Fadel, V., Canduri, F., Dellamano, M., De Azevedo Jr, W. F., Bonilla-Rodriguez, G. O.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.12.2000
• Subjects: Adenosine Triphosphate - metabolism; Animals; carboxyhaemoglobin; Crystallization; Crystallography, X-Ray; Fishes; haemoglobin; Hemoglobins; Hemoglobins, Abnormal - chemistry; Hemoglobins, Abnormal - isolation & purification; Hemoglobins, Abnormal - metabolism; Protein Conformation
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444900015262

Haemoglobin, the `honorary enzyme' [Brunori (1999), Trends Biochem. Sci.24, 158–161], constitutes a prime prototype for allosteric models. Here, the crystallization and preliminary X‐ray analysis of haemoglobin I from the South American fish Brycon cephalus are reported. X‐ray diffraction data have been collected to 2.5 Å resolution using synchrotron radiation (LNLS). Crystals were determined to belong to the space group P6122 and preliminary structural analysis revealed the presence of one dimer (αβ) in the asymmetric unit. The structure was determined using standard molecular‐replacement techniques.