Probing protein fine structures by wide angle solution X-ray scattering

In this report we have investigated the use of wide angle scattering data not only to resolve overall size and shape of protein molecules in solution, but also to resolve details of fine structure. Methods have been developed for calculating protein solution scattering profiles based on atomic coord...

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Bibliographic Details
Published in:Journal of applied crystallography 2000-06, Vol.33 (3-1), p.565-568
Main Authors: Zhang, R., Thiyagarajan, P., Tiede, D.M.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Proteins
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Summary:In this report we have investigated the use of wide angle scattering data not only to resolve overall size and shape of protein molecules in solution, but also to resolve details of fine structure. Methods have been developed for calculating protein solution scattering profiles based on atomic coordinates over a wide range of q with high accuracy in order to compare protein atomic models to wide angle scattering data. Calculations based upon these procedures show that X‐ray scattering profiles for X‐ray crystal and NMR solution structures for cytochrome c are significantly different, and that these differences can be resolved by high‐precision wide angle X‐ray scattering measurements. It is also shown that wide angle X‐ray scattering profiles are rather sensitive to atomic fluctuations (Debye‐Waller temperature factors), suggesting that wide angle scattering data may provide an opportunity for evaluation of protein dynamics.
ISSN:1600-5767
0021-8898
1600-5767
DOI:10.1107/S0021889800001345