Abstract

Human platelet factor 4 was crystallized with ammonium sulfate. The crystals were orthorhombic, space group P21212, with unit cell dimensions a = 78.7 A, b = 80.6 A, and c = 54.6 A. Unit cell volume and mass of the protein (7800 daltons) indicated four or five molecules in each asymmetric unit cell.

Highlights

  • Human platelet factor 4 was crystallized with ammonium sulfate

  • The crystals were transferred to an 80% saturated ammonium sulfate solution and mounted in thin walled glass capillaries in the usual manner

  • Several lysine residues are present in the COOH-terminal portion of the molecule, suggesting that this region may be important in heparin binding

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Summary

Introduction

Human platelet factor 4 was crystallized with ammonium sulfate. The crystals were orthorhombic, space grou P21212, with unit cell dimensions a = 78.7 A, b = Unit cell volume and mass of the protein (7800 daltons) indicated four or five molecules in each asymmetric unit cell. The crystals were transferred to an 80% saturated ammonium sulfate solution and mounted in thin walled glass capillaries in the usual manner.

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