Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
19/04/2012
19/04/2012
2010
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Resumo |
This paper describes a new and simple method to determine the molecular weight of proteins in dilute solution, with an error smaller than similar to 10%, by using the experimental data of a single small-angle X-ray scattering (SAXS) curve measured on a relative scale. This procedure does not require the measurement of SAXS intensity on an absolute scale and does not involve a comparison with another SAXS curve determined from a known standard protein. The proposed procedure can be applied to monodisperse systems of proteins in dilute solution, either in monomeric or multimeric state, and it has been successfully tested on SAXS data experimentally determined for proteins with known molecular weights. It is shown here that the molecular weights determined by this procedure deviate from the known values by less than 10% in each case and the average error for the test set of 21 proteins was 5.3%. Importantly, this method allows for an unambiguous determination of the multimeric state of proteins with known molecular weights. CNPq (Brazil) FAPESP (Sao Paulo, Brazil) |
Identificador |
JOURNAL OF APPLIED CRYSTALLOGRAPHY, v.43, p.101-109, 2010 0021-8898 http://producao.usp.br/handle/BDPI/16626 10.1107/S0021889809043076 |
Idioma(s) |
eng |
Publicador |
WILEY-BLACKWELL PUBLISHING, INC |
Relação |
Journal of Applied Crystallography |
Direitos |
closedAccess Copyright WILEY-BLACKWELL PUBLISHING, INC |
Palavras-Chave | #LOW-RESOLUTION STRUCTURES #ABSOLUTE INTENSITIES #CRYSTAL-STRUCTURES #ESCHERICHIA-COLI #COMPLEX #DIMERS #Crystallography |
Tipo |
article original article publishedVersion |