The Structure of Sickling Deer Type III Hemoglobin by Molecular Replacement

Author(s)

William C. Schmidt Jr., University of South Carolina - ColumbiaFollow
R. L. Girling, University of South Carolina - Columbia
T. E. Houston, University of South Carolina - Columbia
Gordon Sproul, University of South Carolina - Beaufort
E. L. Amma, University of South Carolina - Columbia
T. H. Huisman, Medical College of Georgia

Document Type

Article

Subject Area(s)

chemistry, natural sciences

Abstract

A combination of oriented single-crystal electron microscopy and protein crystallography has been used to show that crystalline sickling deer hemoglobin molecules from Odocoileusvirginianus[oxy fl-chain variant- type III, Hb(DIII)] pack to form a distorted honeycomb (hexagonal) structure with open solvent channels. This network of molecules, consisting of out-of-register anti-parallel strands (fibrils), bears an unmistakable relation to the hemoglobin fibers and aggregates found in human sickled cells. The crystal structure was solved by means of the rotation and translation functions, with data to 3-5/k resolution giving the current residual of 0.430. Oxy- or cyanomet-Hb(DIII) crystallizes in space group C2 with a = 163.49 (3), b = 70.83 (2), c= 65.95 (2) A,fl = 94.15 (1)° and Z = 4.

Publication Info

Published in Acta Crystallographica, Volume B, Issue 33, 1977, pages 335-343.

© Acta Crystallographica 1977, International Union of Crystallography.

Schmidt, W. C., Girling, R. L., Houston, T. E., Sproul, G. D., Amma, E. L. & Huisman, T. H. J. (1977). The structure of sickling deer type III hemoglobin by molecular replacement. Acta Crystallographica, B(33), 335-343. https://doi.org/10.1107/S056774087700363X