Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale


Autoria(s): FISCHER, H.; OLIVEIRA NETO, M. de; NAPOLITANO, H. B.; POLIKARPOV, I.; CRAIEVICH, A. F.
Contribuinte(s)

UNIVERSIDADE DE SÃO PAULO

Data(s)

19/04/2012

19/04/2012

2010

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

http://dx.doi.org/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