Rational 'correction' of the amino-acid sequence of RbcX protein from the thermophilic cyanobacterium Thermosynechococcus elongatus dramatically improves crystallization.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 64(Pt 9): 870-4, 2008 Sep 01.
Article
en En
| MEDLINE
| ID: mdl-18765926
ABSTRACT
RbcX is a dimeric protein found in cyanobacteria that assists in the assembly of the oligomeric RuBisCO complex. RbcX from the thermophile Thermosynechococcus elongatus (TeRbcX) contains an unusual Cys103 residue in its sequence and when expressed recombinantly the protein aggregates and cannot be crystallized. Site-directed mutagenesis of Cys103 to either Arg or Ala produced non-aggregating proteins that could be readily crystallized in several crystal forms. Synchrotron-radiation X-ray diffraction data were collected to 1.96 A resolution and formed the basis of crystal structure analysis of TeRbcX.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
Mutagénesis Sitio-Dirigida
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Cianobacterias
/
Chaperonas Moleculares
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2008
Tipo del documento:
Article
País de afiliación:
Polonia