UNIT 17.4 Crystallization of Macromolecules

  1. Troy Messick,
  2. Ronen Marmorstein

Published Online: 1 FEB 2004

DOI: 10.1002/0471140864.ps1704s34

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Messick, T. and Marmorstein, R. 2004. Crystallization of Macromolecules. Current Protocols in Protein Science. 34:17.4:17.4.1–17.4.25.

Author Information

  1. The Wistar Institute, Philadelphia, Pennsylvania

Publication History

  1. Published Online: 1 FEB 2004
  2. Published Print: NOV 2003

This is not the most recent version of the article. View current version (1 NOV 2011)


X-ray crystallography has evolved into a very powerful tool to determine the three-dimensional structure of macromolecules and macromolecular complexes. The major bottleneck in structure determination by X-ray crystallography is the preparation of suitable crystalline samples. This unit outlines steps for the crystallization of a macromolecule, starting with a purified, homogeneous sample. The first protocols describe preparation of the macromolecular sample (i.e., proteins, nucleic acids, macromolecular complexes, and membrane proteins). The preparation and assessment of crystallization trials is then described, along with a protocol for determining whether the crystals obtained are composed of macromolecule or salt. Next, the optimization of crystallization conditions is presented. Finally, protocols that facilitate the growth of larger crystals through seeding are described.