Related ArticlesHow do the x-ray structure and the NMR structure of FMN-binding protein differ?
Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):368-71
Authors: Suto K, Kawagoe K, Shibata N, Morimoto Y, Higuchi Y, Kitamura M, Nakaya T, Yasuoka N
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 between the two monomers. In particular, Leu122 in the C-terminus has a close contact with the o-xylene moiety of FMN, while solvent molecules may cover the o-xylene moiety in the solution structure.
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How do the x-ray structure and the NMR structure of FMN-binding protein differ?
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