Unknown

Dataset Information

0

Crystallization and preliminary X-ray structural analysis of nucleoside triphosphate hydrolases from Neospora caninum and Toxoplasma gondii.


ABSTRACT: The nucleoside triphosphate hydrolases that are produced by Neospora caninum (NcNTPase) and Toxoplasma gondii (TgNTPase-I) have a different physiological function from the ubiquitous ecto-ATPases. The recombinant enzymes were crystallized at 293?K using polyethylene glycol 3350 as a precipitant and X-ray diffraction data sets were collected for NcNTPase (to 2.8?Å resolution) and TgNTPase-I (to 3.1?Å resolution) at 100?K using synchrotron radiation. The crystals of NcNTPase and TgNTPase-I belonged to the orthorhombic space group I222 (unit-cell parameters a = 93.6, b = 140.8, c = 301.1?Å) and the monoclinic space group P2(1) (unit-cell parameters a = 87.1, b = 123.5, c = 120.2?Å, ? = 96.6°), respectively, with two NcNTPase (V(M) = 3.7?Å(3)?Da(-1)) and four TgNTPase-I (V(M) = 2.7?Å(3)?Da(-1)) molecules per asymmetric unit. SAD phasing trials using a data set (? = 0.97904?Å) collected from a crystal of selenomethionylated NcNTPase gave an initial electron-density map of sufficient quality to build a molecular model of NcNTPase.

SUBMITTER: Matoba K 

PROVIDER: S-EPMC3001644 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystallization and preliminary X-ray structural analysis of nucleoside triphosphate hydrolases from Neospora caninum and Toxoplasma gondii.

Matoba Kazuaki K   Shiba Tomoo T   Takeuchi Tsutomu T   Sibley L David LD   Seiki Makiko M   Kikyo Fumi F   Horiuchi Toshio T   Asai Takashi T   Harada Shigeharu S  

Acta crystallographica. Section F, Structural biology and crystallization communications 20101028 Pt 11


The nucleoside triphosphate hydrolases that are produced by Neospora caninum (NcNTPase) and Toxoplasma gondii (TgNTPase-I) have a different physiological function from the ubiquitous ecto-ATPases. The recombinant enzymes were crystallized at 293 K using polyethylene glycol 3350 as a precipitant and X-ray diffraction data sets were collected for NcNTPase (to 2.8 Å resolution) and TgNTPase-I (to 3.1 Å resolution) at 100 K using synchrotron radiation. The crystals of NcNTPase and TgNTPase-I belonge  ...[more]

Similar Datasets

| S-EPMC4692086 | biostudies-literature
| PRJNA638608 | ENA
| S-EPMC4936363 | biostudies-literature
| S-EPMC4057265 | biostudies-literature
| S-EPMC7093116 | biostudies-literature
| S-EPMC6950991 | biostudies-literature
| S-EPMC7653309 | biostudies-literature
| S-EPMC6568018 | biostudies-literature
| S-EPMC3270962 | biostudies-literature
| S-EPMC7142529 | biostudies-literature