Purification and crystallization of the entire recombinant subunit E of the energy producer A(1)A(o) ATP synthase.
A(1)A(o) ATP synthases are the major energy producers in archaea. Subunit E of the stator domain of the ATP synthase from Pyrococcus horikoshii OT3 was cloned, expressed and purified to homogeneity. The monodispersed protein was crystallized by vapour diffusion. A complete diffraction data set was collected to 3.3 A resolution with 99.4% completeness using a synchrotron-radiation source. The crystals belonged to space group I4, with unit-cell parameters a = 112.51, b = 112.51, c = 96.25 A, and contained three molecules in the asymmetric unit.
Balakrishna
Asha Manikkoth
AM
Nanyang Technological University, School of Biological Sciences, 60 Nanyang Drive, Singapore 637551, Singapore.
Hunke
Cornelia
C
Grüber
Gerhard
G
D025181:ATP Synthetase Complexes / Q000737:chemistry* / Q000302:isolation & purification; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D021122:Protein Subunits / Q000737:chemistry / Q000302:isolation & purification; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D021122:Protein Subunits; D011994:Recombinant Proteins; D025181:ATP Synthetase Complexes