NMR structure of the protein NP-247299.1: Comparison with the crystal structure

Kristaps Jaudzems, Michael Geralt, Pedro Serrano, Biswaranjan Mohanty, Reto Horst, Bill Pedrini, Marc André Elsliger, Ian A Wilson, Kurt Wüthrich

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The NMR structure of the protein NP-247299.1 in solution at 313 K has been determined and is compared with the X-ray crystal structure, which was also solved in the Joint Center for Structural Genomics (JCSG) at 100 K and at 1.7 Å resolution. Both structures were obtained using the current largely automated crystallographic and solution NMR methods used by the JCSG. This paper assesses the accuracy and precision of the results from these recently established automated approaches, aiming for quantitative statements about the location of structure variations that may arise from either one of the methods used or from the different environments in solution and in the crystal. To evaluate the possible impact of the different software used for the crystallographic and the NMR structure determinations and analysis, the concept is introduced of reference structures, which are computed using the NMR software with input of upper-limit distance constraints derived from the molecular models representing the results of the two structure determinations. The use of this new approach is explored to quantify global differences that arise from the different methods of structure determination and analysis versus those that represent interesting local variations or dynamics. The near-identity of the protein core in the NMR and crystal structures thus provided a basis for the identification of complementary information from the two different methods. It was thus observed that locally increased crystallographic B values correlate with dynamic structural polymorphisms in solution, including that the solution state of the protein involves a slow dynamic equilibrium on a time scale of milliseconds or slower between two ensembles of rapidly interchanging conformers that contain, respectively, the cis or trans form of the C-terminal proline and represent about 25 and 75% of the total protein.

Original languageEnglish
Pages (from-to)1367-1380
Number of pages14
JournalActa Crystallographica Section F: Structural Biology Communications
Issue number10
Publication statusPublished - Oct 2010
Externally publishedYes


  • nitrogenase iron-molybdenum cofactor
  • reference structures
  • structure comparison in crystals and in solution
  • structure-determination software

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