Crystallization and preliminary crystallographic analysis of human glycosylated haemoglobin

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2006-02, Vol.62 (2), p.106-109
• Main Authors: Syakhovich, Vitaly E., Saraswathi, N. T., Ruff, Marc, Bokut, Sergey B., Moras, Dino
• Format: Article
• Language: English
• Subjects: Biochemistry, Molecular Biology; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; Crystallization Communications; Crystallography, X-Ray; CRYSTALS; DIFFRACTION; DIFFUSION; GLUCOSE; Glycated Hemoglobin A - chemistry; Glycated Hemoglobin A - metabolism; glycosylation; haemoglobin; HEMOGLOBIN; Hemoglobin A, Glycosylated; Humans; IN VIVO; Life Sciences; MODIFICATIONS; Molecular biology; MOLECULES; RESOLUTION; SOLVENTS; SPACE GROUPS; WEIGHT
• ISSN: 1744-3091; 2053-230X; 1744-3091; 2053-230X
• DOI: 10.1107/S1744309105042764

Human glycosylated haemoglobin A1C is a stable minor variant formed in vivo by post‐translational modification of the main form of haemoglobin by glucose. Crystals of oxyHbA1C were obtained using the hanging‐drop vapour‐diffusion method and PEG as precipitant. The diffraction pattern of the crystal extends to a resolution of 2.3 Å at 120 K. The crystals belong to space group C2, with unit‐cell parameters a = 237.98, b = 59.27, c = 137.02 Å, α = 90.00, β = 125.40, γ = 90.00°. The presence of two and a half molecules per asymmetric unit gives a crystal volume per protein weight (VM) of 9.70 Å3 Da−1 and a solvent content of 49%.