Unknown

Dataset Information

0

Rational 'correction' of the amino-acid sequence of RbcX protein from the thermophilic cyanobacterium Thermosynechococcus elongatus dramatically improves crystallization.


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.

SUBMITTER: Tarnawski M 

PROVIDER: S-EPMC2531263 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Rational 'correction' of the amino-acid sequence of RbcX protein from the thermophilic cyanobacterium Thermosynechococcus elongatus dramatically improves crystallization.

Tarnawski Miroslaw M   Krzywda Szymon S   Szczepaniak Andrzej A   Jaskolski Mariusz M  

Acta crystallographica. Section F, Structural biology and crystallization communications 20080829 Pt 9


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 diffrac  ...[more]

Similar Datasets

| S-EPMC3151113 | biostudies-literature
| S-EPMC3433194 | biostudies-literature
| S-EPMC2878562 | biostudies-literature
| S-EPMC3607189 | biostudies-literature
| S-EPMC451613 | biostudies-literature
| S-EPMC4180030 | biostudies-literature
| S-EPMC8091003 | biostudies-literature
| S-EPMC2943282 | biostudies-literature
| S-EPMC3907722 | biostudies-literature
| S-EPMC1170355 | biostudies-other