Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin. I. 0.69 Å X-ray structure of mutant W4L/R5S

Heiko Bönisch*, Christian L. Schmidt, Pierre Bianco, Rudolf Ladenstein

*Corresponding author for this work
30 Citations (Scopus)


The crystal structure of Pyrococcus abyssi rubredoxin mutant W4L/R5S was solved by direct methods. The model of the air-oxidized protein was refined by partially restrained full-matrix least-squares refinement against intensity data to 0.69 Å resolution. This first ultrahigh-resolution structure of a rubredoxin provides very detailed and precise information about the Fe(SCys)4 centre and its environment, the peptide-backbone stereochemistry, H atoms and hydrogen bonds, static and dynamic disorder, the solvent structure and the electron-density distribution. P. abyssi rubredoxin W4L/R5S is the first of a series of mutants studied by atomic and ultrahigh-resolution X-ray crystallography which are expected to contribute to the understanding of structure-function relationships in iron-sulfur proteins.

Original languageEnglish
JournalActa Crystallographica Section D: Biological Crystallography
Issue number7
Pages (from-to)990-1004
Number of pages15
Publication statusPublished - 01.07.2005

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


Dive into the research topics of 'Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin. I. 0.69 Å X-ray structure of mutant W4L/R5S'. Together they form a unique fingerprint.

Cite this