Control of nucleation of protein crystals

Protein Sci. 1994 Oct;3(10):1638-43. doi: 10.1002/pro.5560031003.

Abstract

Control of nucleation may be needed to obtain a reliable supply of large protein crystals, when standard techniques give many small or twinned crystals. Heterogeneous nucleation may be controlled by the use of fine filters, with the elimination of airborne contaminants by working under paraffin oil. The area of contact with the supporting vessel also has an important effect. A heterogenous nucleant for lysozyme (identified earlier) has been shown to be effective for carboxypeptidase G2. Control of homogeneous nucleation (previously demonstrated by dilutions of a nucleating sample after various times of incubation) may also be achieved by incubating a sample at 1 temperature, where nucleation can occur, and changing the temperature to conditions where there is growth but no nucleation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chemical Phenomena
  • Chemistry, Physical
  • Crystallization
  • Filtration / instrumentation
  • Muramidase / chemistry
  • Paraffin
  • Polyethylene Glycols
  • Proteins / chemistry*
  • Temperature
  • gamma-Glutamyl Hydrolase / chemistry

Substances

  • Proteins
  • Polyethylene Glycols
  • Paraffin
  • Muramidase
  • gamma-Glutamyl Hydrolase