Crystallization and preliminary X-ray characterization of the acylphosphatase-like domain from the Escherichia coli hydrogenase maturation factor HypF

Camillo Rosano, Simone Zuccotti, Massimo Stefani, Monica Bucciantini, Giampietro Ramponi, Martino Bolognesi

Research output: Contribution to journalArticle


Maturation of prokaryotic hydrogenase involves several protein factors, among which is the accessory protein HypF, which hosts the consensus sequence of acylphosphatases and a sequence motif common to proteins catalyzing O-carbamoylations. The specific functions of HypF are largely unknown, although it has been observed that CN- and CO ligands at the hydrogenase Ni,Fe active centre originate from carbamoylphosphate. The HypF N-terminal domain (91 residues, acylphosphatase-like domain) has been crystallized in two different crystal forms belonging to the orthorhombic P212121 space group (unit-cell parameters a = 35.5, b = 59.8, c = 87.6 Å) and to the rhombohedral space group R32 (unit-cell parameters a = b = 58.1, c = 155.6 Å in the hexagonal setting).

Original languageEnglish
Pages (from-to)524-525
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Issue number3
Publication statusPublished - 2002


ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Clinical Biochemistry
  • Structural Biology
  • Condensed Matter Physics

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