Crystallization of the flavoprotein WrbA optimized by using additives and gels

Julie Wolfova, Rita Grandori, Erika Kozma, Neal Chatterjee, Jannette Carey, Ivana Kuta Smatanova

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


The tryptophan (W)-repressor binding protein A (WrbA) identified as an Escherichia coli stationary-phase protein was proposed as the founding member of a new family of multimeric flavodoxin-like proteins implicated in oxidative-stress defense. Since WrbA is largely uncharacterized with respect to both molecular and physiological functions, the present effort is aimed at structural characterization. WrbA apoprotein was purified and used for crystallization trials at room temperature. Multicrystals of WrbA apoprotein were obtained using standard and advanced crystallization techniques. Application of additives and gelling protein for crystallization in single capillaries yielded diffraction-quality single crystals. The crystals diffracted to a resolution of 2.2 Å at synchrotrons DESY (X13) in Hamburg (Germany), and Elletra (XRD1) in Trieste (Italy).

Original languageEnglish (US)
Pages (from-to)502-505
Number of pages4
JournalJournal of Crystal Growth
Issue number3-4
StatePublished - Nov 1 2005

All Science Journal Classification (ASJC) codes

  • Condensed Matter Physics
  • Inorganic Chemistry
  • Materials Chemistry


  • A1. Biocrystallization
  • A1. Optimization of crystallization
  • A2. Single crystal growth
  • B1. Additives


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