Promoting protein crystallization using a plate with simple geometry

Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):647-57. doi: 10.1107/S1399004713032100. Epub 2014 Feb 15.

Abstract

Increasing the probability of obtaining protein crystals in crystallization screening is always an important goal for protein crystallography. In this paper, a new method called the cross-diffusion microbatch (CDM) method is presented, which aims to efficiently promote protein crystallization and increase the chance of obtaining protein crystals. In this method, a very simple crystallization plate was designed in which all crystallization droplets are in one sealed space, so that a variety of volatile components from one droplet can diffuse into any other droplet via vapour diffusion. Crystallization screening and reproducibility tests indicate that this method could be a potentially powerful technique in practical protein crystallization screening. It can help to obtain crystals with higher probability and at a lower cost, while using a simple and easy procedure.

Keywords: cross-diffusion microbatch method; crystallization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyltransferases / chemistry
  • Acetyltransferases / genetics
  • Animals
  • Catalase / chemistry
  • Chickens
  • Chymotrypsinogen / chemistry
  • Concanavalin A / chemistry
  • Crystallization / economics
  • Crystallization / methods*
  • Muramidase / chemistry
  • Proteins / chemistry*
  • Proteins / economics
  • Recombinant Proteins / chemistry
  • Reproducibility of Results

Substances

  • Proteins
  • Recombinant Proteins
  • Concanavalin A
  • Chymotrypsinogen
  • Catalase
  • Acetyltransferases
  • homoserine O-acetyltransferase
  • hen egg lysozyme
  • Muramidase