Comparison of the solution nuclear magnetic resonance and X-ray crystal structures of human recombinant interleukin-1 beta.
The solution structure of interleukin-1 beta determined by nuclear magnetic resonance spectroscopy is compared to three independently solved X-ray structures at 2 A resolution. It is shown that the solution and X-ray structures are very similar, both locally and globally. The atomic root-mean-square (r.m.s.) difference between the solution and X-ray structures is approximately 0.9 A for backbone atoms, approximately 1.5 A for all atoms and approximately 1 A for all atoms of internal residues. The largest differences are confined to some of the loops and turns connecting beta-strands. The atomic r.m.s. distribution of the 32 calculated solution structures about their mean co-ordinate positions (approximately 0.4 A for backbone atoms, approximately 0.8 A for all atoms and approximately 0.5 A for all atoms of internal residues) is approximately the same as the atomic r.m.s. differences between the three X-ray structures, indicating that the positional errors in the atomic co-ordinates determined by the two methods are similar.
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda,MD 20892.
G M
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Clore
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Gronenborn
D006801:Humans; D007375:Interleukin-1 / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D011994:Recombinant Proteins / Q000737:chemistry; D012996:Solutions; D013816:Thermodynamics; D014961:X-Ray Diffraction
D007375:Interleukin-1; D011994:Recombinant Proteins; D012996:Solutions