Structure determination of an integral membrane protein at room temperature from crystals in situ.
Acta Crystallogr D Biol Crystallogr
; 71(Pt 6): 1228-37, 2015 Jun.
Article
en En
| MEDLINE
| ID: mdl-26057664
The structure determination of an integral membrane protein using synchrotron X-ray diffraction data collected at room temperature directly in vapour-diffusion crystallization plates (in situ) is demonstrated. Exposing the crystals in situ eliminates manual sample handling and, since it is performed at room temperature, removes the complication of cryoprotection and potential structural anomalies induced by sample cryocooling. Essential to the method is the ability to limit radiation damage by recording a small amount of data per sample from many samples and subsequently assembling the resulting data sets using specialized software. The validity of this procedure is established by the structure determination of Haemophilus influenza TehA at 2.3â
Å resolution. The method presented offers an effective protocol for the fast and efficient determination of membrane-protein structures at room temperature using third-generation synchrotron beamlines.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Cristalografía por Rayos X
/
Proteínas de la Membrana
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Año:
2015
Tipo del documento:
Article
País de afiliación:
Reino Unido
Pais de publicación:
Estados Unidos