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

@article{citeulike:1074836, abstract = {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.}, address = {Department of Life Science, Faculty of Science, Himeji Institute of Technology, 3-2-1 Kouto, Kamigori Ako-gun, Hyogo 678-1297, Japan.}, author = {Suto, K. and Kawagoe, K. and Shibata, N. and Morimoto, Y. and Higuchi, Y. and Kitamura, M. and Nakaya, T. and Yasuoka, N. }, citeulike-article-id = {1074836}, issn = {0907-4449}, journal = {Acta Crystallogr D Biol Crystallogr}, keywords = {jcsg, pdb-1flm, scop-b-45-1-1, split-barrel}, month = {March}, number = {Pt 3}, pages = {368--371}, posted-at = {2007-01-29 19:17:59}, priority = {2}, title = {How do the x-ray structure and the NMR structure of FMN-binding protein differ?}, url = {http://view.ncbi.nlm.nih.gov/pubmed/10713530}, volume = {56}, year = {2000} }

TY - JOUR ID - citeulike:1074836 L3 - citeulike-article-id:1074836 TI - How do the x-ray structure and the NMR structure of FMN-binding protein differ? JF - Acta Crystallogr D Biol Crystallogr VL - 56 IS - Pt 3 SP - 368 EP - 371 AD - Department of Life Science, Faculty of Science, Himeji Institute of Technology, 3-2-1 Kouto, Kamigori Ako-gun, Hyogo 678-1297, Japan. SN - 0907-4449 N2 - 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. KW - jcsg KW - pdb-1flm KW - scop-b-45-1-1 KW - split-barrel AU - Suto, K AU - Kawagoe, K AU - Shibata, N AU - Morimoto, Y AU - Higuchi, Y AU - Kitamura, M AU - Nakaya, T AU - Yasuoka, N PY - 2000/03// UR - http://view.ncbi.nlm.nih.gov/pubmed/10713530 ER -