Unknown

Dataset Information

0

Overexpression, purification, crystallization and preliminary X-ray analysis of uracil N-glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor.


ABSTRACT: Uracil N-glycosylase is an enzyme which initiates the pathway of uracil-excision repair of DNA. The enzyme from Mycobacterium tuberculosis was co-expressed with a proteinaceous inhibitor from Bacillus subtilis phage and was crystallized in monoclinic space group C2, with unit-cell parameters a = 201.14, b = 64.27, c = 203.68 A, beta = 109.7 degrees. X-ray data from the crystal have been collected for structure analysis.

SUBMITTER: Singh P 

PROVIDER: S-EPMC2225355 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Overexpression, purification, crystallization and preliminary X-ray analysis of uracil N-glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor.

Singh Prem P   Talawar Ramappa K RK   Krishna P D V PD   Varshney Umesh U   Vijayan M M  

Acta crystallographica. Section F, Structural biology and crystallization communications 20061130 Pt 12


Uracil N-glycosylase is an enzyme which initiates the pathway of uracil-excision repair of DNA. The enzyme from Mycobacterium tuberculosis was co-expressed with a proteinaceous inhibitor from Bacillus subtilis phage and was crystallized in monoclinic space group C2, with unit-cell parameters a = 201.14, b = 64.27, c = 203.68 A, beta = 109.7 degrees. X-ray data from the crystal have been collected for structure analysis. ...[more]

Similar Datasets

| S-EPMC2376397 | biostudies-literature
| S-EPMC3212474 | biostudies-literature
| S-EPMC3433208 | biostudies-literature
| S-EPMC3792668 | biostudies-literature
| S-EPMC3855718 | biostudies-literature
| S-EPMC4304759 | biostudies-literature
| S-EPMC4118811 | biostudies-literature
| S-EPMC3253829 | biostudies-literature
| S-EPMC3370911 | biostudies-literature
| S-EPMC3539705 | biostudies-literature