Increasing the diffraction limit and internal order of a membrane protein crystal by dehydration.
J Struct Biol
; 141(2): 97-102, 2003 Feb.
Article
en En
| MEDLINE
| ID: mdl-12615535
It is notoriously difficult to produce crystals of membrane proteins that diffract to sufficient resolution for structural studies by X-ray crystallography. Crystals of a prokaryotic CLC chloride channel that were initially unacceptable for structural analysis improved in both quality and diffraction limit by a process of dehydration. The loss of water decreased the dimensions of the unit cell axes by up to 25 A, improved the diffraction limit from 8.0 to 4.0 A, and decreased the mosaicity to values of approximately 1 degrees. Dehydration of integral membrane protein crystals should be one of the procedures included in the initial screening for appropriate crystals and as a method of improving the diffraction limits of existing crystals.
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Bases de datos:
MEDLINE
Asunto principal:
Difracción de Rayos X
/
Membrana Celular
/
Cristalografía por Rayos X
Idioma:
En
Revista:
J Struct Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2003
Tipo del documento:
Article