Literature DB >> 16511276

Crystallization and preliminary crystallographic analysis of human glycosylated haemoglobin.

Vitaly E Syakhovich1, N T Saraswathi, Marc Ruff, Sergey B Bokut, Dino Moras.   

Abstract

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 A at 120 K. The crystals belong to space group C2, with unit-cell parameters a = 237.98, b = 59.27, c = 137.02 A, alpha = 90.00, beta = 125.40, gamma = 90.00 degrees. The presence of two and a half molecules per asymmetric unit gives a crystal volume per protein weight (VM) of 9.70 A3 Da(-1) and a solvent content of 49%.

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Year:  2006        PMID: 16511276      PMCID: PMC2150954          DOI: 10.1107/S1744309105042764

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  18 in total

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5.  Age-related changes in collagen: the identification of reducible lysine-carbohydrate condensation products.

Authors:  S P Robins; A J Bailey
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6.  Studies on the heterogeneity of hemoglobin. IX. The use of Tris(hydroxymethyl)aminomethanehcl buffers in the anion-exchange chromatography of hemoglobins.

Authors:  T H Huisman; A M Dozy
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Authors:  J W Baynes; H F Bunn; D Goldstein; M Harris; D B Martin; C Peterson; K Winterhalter
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Authors:  C E Guthrow; M A Morris; J F Day; S R Thorpe; J W Baynes
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10.  Effect of phosphate on the kinetics and specificity of glycation of protein.

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