Unknown

Dataset Information

0

Overproduction, purification, crystallization and preliminary X-ray diffraction analysis of Trypanosoma brucei gambiense glycerol kinase.


ABSTRACT: In the bloodstream forms of human trypanosomes, glycerol kinase (GK; EC 2.7.1.30) is one of the nine glycosomally compartmentalized enzymes that are essential for energy metabolism. In this study, a recombinant Trypanosoma brucei gambiense GK (rTbgGK) with an N-terminal cleavable His(6) tag was overexpressed, purified to homogeneity and crystallized by the sitting-drop vapour-diffusion method using PEG 400 as a precipitant. A complete X-ray diffraction data set to 2.75 A resolution indicated that the crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 63.84, b = 121.50, c = 154.59 A. The presence of two rTbgGK molecules in the asymmetric unit gives a Matthews coefficient (V(M)) of 2.5 A(3) Da(-1), corresponding to 50% solvent content.

SUBMITTER: Balogun EO 

PROVIDER: S-EPMC2833043 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Overproduction, purification, crystallization and preliminary X-ray diffraction analysis of Trypanosoma brucei gambiense glycerol kinase.

Balogun Emmanuel Oluwadare EO   Inaoka Daniel Ken DK   Kido Yasutoshi Y   Shiba Tomoo T   Nara Takeshi T   Aoki Takashi T   Honma Teruki T   Tanaka Akiko A   Inoue Masayuki M   Matsuoka Shigeru S   Michels Paul A M PA   Harada Shigeharu S   Kita Kiyoshi K  

Acta crystallographica. Section F, Structural biology and crystallization communications 20100224 Pt 3


In the bloodstream forms of human trypanosomes, glycerol kinase (GK; EC 2.7.1.30) is one of the nine glycosomally compartmentalized enzymes that are essential for energy metabolism. In this study, a recombinant Trypanosoma brucei gambiense GK (rTbgGK) with an N-terminal cleavable His(6) tag was overexpressed, purified to homogeneity and crystallized by the sitting-drop vapour-diffusion method using PEG 400 as a precipitant. A complete X-ray diffraction data set to 2.75 A resolution indicated tha  ...[more]

Similar Datasets

| S-EPMC2688435 | biostudies-literature
| S-EPMC3729160 | biostudies-literature
| S-EPMC2219979 | biostudies-literature
| S-EPMC2496858 | biostudies-literature
| S-EPMC2675601 | biostudies-literature
| S-EPMC3253832 | biostudies-literature
| S-EPMC3080155 | biostudies-literature
| S-EPMC2765893 | biostudies-literature
| S-EPMC3079970 | biostudies-literature
| S-EPMC2998380 | biostudies-literature