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 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.
journal_name
J Biomol NMRjournal_title
Journal of biomolecular NMRauthors
Raves ML,Doreleijer JF,Vis H,Vorgias CE,Wilson KS,Kaptei Rdoi
10.1023/a:1012927325963subject
Has Abstractpub_date
2001-11-01 00:00:00pages
235-48issue
3eissn
0925-2738issn
1573-5001journal_volume
21pub_type
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