Unknown

Dataset Information

0

Crystallization and preliminary crystallographic analysis of DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase from Corynebacterium glutamicum.


ABSTRACT: DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase derived from Corynebacterium glutamicum, was crystallized by the sitting-drop vapour-diffusion method using polyethylene glycol 6000 as a precipitant. The crystal belongs to the trigonal system with space group R32 and contains three subunits in the asymmetric unit. A molecular-replacement solution was found using the structure of transcarboxylase 12S from Propionibacterium shermanii as a search model.

SUBMITTER: Yamada M 

PROVIDER: S-EPMC2330119 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystallization and preliminary crystallographic analysis of DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase from Corynebacterium glutamicum.

Yamada Minoru M   Natsume Ryo R   Nakamatsu Tsuyoshi T   Horinouchi Sueharu S   Kawasaki Hisashi H   Senda Toshiya T  

Acta crystallographica. Section F, Structural biology and crystallization communications 20070127 Pt 2


DtsR1, a carboxyltransferase subunit of acetyl-CoA carboxylase derived from Corynebacterium glutamicum, was crystallized by the sitting-drop vapour-diffusion method using polyethylene glycol 6000 as a precipitant. The crystal belongs to the trigonal system with space group R32 and contains three subunits in the asymmetric unit. A molecular-replacement solution was found using the structure of transcarboxylase 12S from Propionibacterium shermanii as a search model. ...[more]

Similar Datasets

| S-EPMC3668587 | biostudies-literature
2006-10-07 | GSE5977 | GEO
| S-EPMC2533188 | biostudies-literature