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Title: Crystallization and preliminary crystallographic analysis of human glycosylated haemoglobin

Abstract

Non enzymatic modification of haemoglobin by glucose plays an important role in diabetes pathogenesis. Here the purification, characterization and crystallization of human glycosylated haemoglobin are reported. Human glycosylated haemoglobin A{sub 1C} is a stable minor variant formed in vivo by post-translational modification of the main form of haemoglobin by glucose. Crystals of oxyHbA{sub 1C} 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 (V{sub M}) of 9.70 Å{sup 3} Da{sup −1} and a solvent content of 49%.

Authors:
 [1]; ;  [2];  [1];  [2];  [3]
  1. Department of Biochemistry and Biophysics, International Sakharov Environmental University, Dolgobrodskaya St 23, 220009 Minsk (Belarus)
  2. Département de Biologie et Génomique Structurales, Institut de Génétique et de Biologie Moléculaire et Cellulaire, 1 Rue Laurent Fries, BP 10142, 67404 Illkirch (France)
  3. (Belarus)
Publication Date:
OSTI Identifier:
22356266
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 2; Other Information: PMCID: PMC2150954; PMID: 16511276; PUBLISHER-ID: ll5032; OAI: oai:pubmedcentral.nih.gov:2150954; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFRACTION; DIFFUSION; GLUCOSE; HEMOGLOBIN; IN VIVO; MODIFICATIONS; MOLECULES; RESOLUTION; SOLVENTS; SPACE GROUPS; WEIGHT

Citation Formats

Syakhovich, Vitaly E., Saraswathi, N. T., Ruff, Marc, E-mail: ruff@igbmc.u-strasbg.fr, Bokut, Sergey B., Moras, Dino, and Department of Biochemistry and Biophysics, International Sakharov Environmental University, Dolgobrodskaya St 23, 220009 Minsk. Crystallization and preliminary crystallographic analysis of human glycosylated haemoglobin. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309105042764.
Syakhovich, Vitaly E., Saraswathi, N. T., Ruff, Marc, E-mail: ruff@igbmc.u-strasbg.fr, Bokut, Sergey B., Moras, Dino, & Department of Biochemistry and Biophysics, International Sakharov Environmental University, Dolgobrodskaya St 23, 220009 Minsk. Crystallization and preliminary crystallographic analysis of human glycosylated haemoglobin. United Kingdom. doi:10.1107/S1744309105042764.
Syakhovich, Vitaly E., Saraswathi, N. T., Ruff, Marc, E-mail: ruff@igbmc.u-strasbg.fr, Bokut, Sergey B., Moras, Dino, and Department of Biochemistry and Biophysics, International Sakharov Environmental University, Dolgobrodskaya St 23, 220009 Minsk. Wed . "Crystallization and preliminary crystallographic analysis of human glycosylated haemoglobin". United Kingdom. doi:10.1107/S1744309105042764.
@article{osti_22356266,
title = {Crystallization and preliminary crystallographic analysis of human glycosylated haemoglobin},
author = {Syakhovich, Vitaly E. and Saraswathi, N. T. and Ruff, Marc, E-mail: ruff@igbmc.u-strasbg.fr and Bokut, Sergey B. and Moras, Dino and Department of Biochemistry and Biophysics, International Sakharov Environmental University, Dolgobrodskaya St 23, 220009 Minsk},
abstractNote = {Non enzymatic modification of haemoglobin by glucose plays an important role in diabetes pathogenesis. Here the purification, characterization and crystallization of human glycosylated haemoglobin are reported. Human glycosylated haemoglobin A{sub 1C} is a stable minor variant formed in vivo by post-translational modification of the main form of haemoglobin by glucose. Crystals of oxyHbA{sub 1C} 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 (V{sub M}) of 9.70 Å{sup 3} Da{sup −1} and a solvent content of 49%.},
doi = {10.1107/S1744309105042764},
journal = {Acta Crystallographica. Section F},
number = Pt 2,
volume = 62,
place = {United Kingdom},
year = {Wed Feb 01 00:00:00 EST 2006},
month = {Wed Feb 01 00:00:00 EST 2006}
}