How do the x-ray structure and the NMR structure of FMN-binding protein differ?

@article{Suto2000HowDT,
  title={How do the x-ray structure and the NMR structure of FMN-binding protein differ?},
  author={Kyoko Suto and Kenichi Kawagoe and Naoki Shibata and Yukio Morimoto and Yoshiki Higuchi and Masaya Kitamura and Tadao Nakaya and Noritake Yasuoka},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2000},
  volume={56 Pt 3},
  pages={368-71}
}
The crystal structure of FMN-binding protein (FMN-bp) from Desulfovibrio vulgaris Miyazaki F was solved by the multiple isomorphous replacement method and refined to an R factor of 15.1% at 1.3 A resolution. FMN-bp exists in a dimeric form in the crystal, in contrast to the monomeric structure determined by NMR. R.m.s. deviations between the crystal structure and the solution structure are more than 2 A, which implies significant differences. There are some hydrophobic residues in the interface… CONTINUE READING

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