Purification, crystallization and preliminary X-ray diffraction studies of parakeet (Psittacula krameri) haemoglobin

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 65; no. 10; pp. 1027 - 1029
• Main Authors: Jaimohan, S. M., Naresh, M. D., Arumugam, V., Mandal, A. B.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01-10-2009
• Subjects: Animals; avian haemoglobin; Crystallization; Crystallization Communications; Crystallography, X-Ray; Hemoglobins - chemistry; Psittacula; Psittacula krameri
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309109034071

Birds often show efficient oxygen management in order to meet the special demands of their metabolism. However, the structural studies of avian haemoglobins (Hbs) are inadequate for complete understanding of the mechanism involved. Towards this end, purification, crystallization and preliminary X‐ray diffraction studies have been carried out for parakeet Hb. Parakeet Hb was crystallized as the met form in low‐salt buffered conditions after extracting haemoglobin from crude blood by microcentrifugation and purifying the sample by column chromatography. Good‐quality crystals were grown from 10% PEG 3350 and a crystal diffracted to about 2.8 Å resolution. Preliminary diffraction data showed that the Hb crystal belonged to the monoclinic system (space group C2), with unit‐cell parameters a = 110.68, b = 64.27, c = 56.40 Å, β = 109.35°. Matthews volume analysis indicated that the crystals contained a half‐tetramer in the asymmetric unit.