Crystals of the hydrogenase maturation factor HypF N-terminal domain grown in microgravity, display improved internal order

Marco Ponassi, Lamberto Felli, Stefania Parodi, Ugo Valbusa, Camillo Rosano

Research output: Contribution to journalArticle

Abstract

Synthesis of the active [NiFe]-hydrogenase in prokaryotes requires a series of ancillary maturation factors. Among them, the HypF maturation factor is a multidomain 82 kDa protein, whose N-terminal domain displays sequence and structural similarities to acylphosphatases. Acylphosphatases are small enzymes that are able to catalyze carboxyl-phosphate bond hydrolysis in acylphosphates, as well as in nucleoside di- and tri-phosphates and in arylphosphates. Here, we present a crystallographic comparison between microgravity and earth-grown crystals of the HypF N-terminal domain. Both crystals were of excellent quality, thereby allowing us to collect very high resolution datasets. A detailed analysis of data collection and refinement statistics, together with an analysis of the diffraction pattern showed that microgravity would appear to further improve the internal order of crystals.

Original languageEnglish
Pages (from-to)246-251
Number of pages6
JournalJournal of Crystal Growth
Volume314
Issue number1
DOIs
Publication statusPublished - Jan 1 2011

Keywords

  • A1. Biocrystallization
  • A1. High resolution X-ray diffraction
  • A1. Microgravity conditions
  • B1. Proteins

ASJC Scopus subject areas

  • Condensed Matter Physics
  • Materials Chemistry
  • Inorganic Chemistry

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