Abstract
Joint refinement, i.e., the simultaneous refinement of a structure against both nuclear magnetic resonance (NMR)
spectroscopic and X-ray crystallographic data, was performed on the HU protein from Bacillus stearothermophilus
(HUBst). The procedurewas aimed at investigating the compatibility of the two data sets and at identifying conflicting
information.Wherever important differences were found, such as peptide flips in the main-chain conformation,
the data were further analyzed to find the cause. The NMR data showed some errors arising either from the manual
interpretation of the spectra or from the incorrect account for spin diffusion. The most important artefact inherent
to the X-ray data is the crystal packing of the molecules: the effects range from the limitation of the freedom of the
flexible parts of the HUBst molecule to possibly one of the peptide flips.
Original language | Undefined/Unknown |
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Pages (from-to) | 235-248 |
Number of pages | 14 |
Journal | Journal of Biomolecular NMR |
Volume | 21 |
Publication status | Published - 2001 |