Joint refinement as a tool for thorough comparison between NMR and X-ray data and structures of HU protein.
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 procedure was 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.
Raves
M L
ML
Department of NMR Spectroscopy, Utrecht University, The Netherlands.
Doreleijer
J F
JF
Vis
H
H
Vorgias
C E
CE
Wilson
K S
KS
Kaptei
R
R
D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D004058:Diffusion; D001411:Geobacillus stearothermophilus / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D015203:Reproducibility of Results; D055672:Static Electricity
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C040330:histone-like protein HU, bacteria