Protein nucleation and crystallization by homologous protein thin film template

J Cell Biochem. 2002;85(2):243-51. doi: 10.1002/jcb.10123.

Abstract

A new method of protein nucleation and crystallization based on Langmuir-Blodgett technology is here utilized for the template stimulation of crystal growth of so far non-crystallized proteins. Microcrystals (60-120 microm) of bovine cytochrome P450scc and human protein kinase CKII alpha subunit were obtained with use of the homologous protein thin film template by vapor diffusion modified hanging drop method. The induction of microcrystals nucleation by the thin template confirms in the two different important classes of proteins, until now never crystallized, the positive stimulatory influence for crystal formation of protein thin film template, which was observed in an earlier study with a model system (chicken egg white lysozyme) as an unexpected acceleration and enhancement in the crystal growth.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Casein Kinase II
  • Cattle
  • Cholesterol Side-Chain Cleavage Enzyme / chemistry*
  • Cholesterol Side-Chain Cleavage Enzyme / ultrastructure
  • Crystallization
  • Crystallography / instrumentation
  • Crystallography / methods
  • Escherichia coli / enzymology
  • Humans
  • Particle Size
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Serine-Threonine Kinases / ultrastructure
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / ultrastructure
  • Volatilization

Substances

  • Recombinant Proteins
  • Cholesterol Side-Chain Cleavage Enzyme
  • Casein Kinase II
  • Protein Serine-Threonine Kinases