Structure determination of a protein assembly by amino acid selective cross-saturation

Eiji Kanamori, Shunsuke Igarashi, Masanori Osawa, Yoshifumi Fukunishi, Ichio Shimada, Haruki Nakamura

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


Amino acid selective cross-saturation (ASCS) method not only provides information about the interface of a protein assembly by the spin relaxation experiment, but also identifies the amino acid residues in the acceptor protein, which are located close to the selectively labeled amino acid residues in the donor protein. Here, a new method was developed to build a precise structural model of a protein assembly, which satisfies the experimental ASCS values, using simulated annealing computation. This method was applied to the ubiquitin-yeast ubiquitin hydrolase 1 (Ub-YUH1) complex to build a precise complex structure compatible with that determined by X-ray crystallography. Proteins 2010.

Original languageEnglish
Pages (from-to)179-190
Number of pages12
JournalProteins: Structure, Function and Bioinformatics
Issue number1
Publication statusPublished - 2011 Jan
Externally publishedYes


  • Cross-saturation
  • Flexible docking
  • Molecular dynamics
  • Nuclear magnetic resonance
  • Protein-protein interaction
  • Ubiquitin

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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