Purification, crystallization and preliminary X-ray analysis of inorganic pyrophosphatase from Thermus thermophilus.
High yields of inorganic pyrophosphatase from Thermus thermophilus HB8 have been purified to homogeneity using anion exchange and hydrophobic chromatography. Crystals suitable for X-ray analysis were obtained by vapour diffusion using ammonium sulphate as precipitant. They belong to the rhombohedral space group R32, with unit cell dimensions a = b = 110.3 A and c = 82.0 A, with one subunit per asymmetric unit. The crystals diffract to 2.0 A resolution.
Obmolova
G
G
Institute of Crystallography, Moscow, Russia.
Kuranova
I
I
Teplyakov
A
A
D001426:Bacterial Proteins / Q000302:isolation & purification / Q000648:ultrastructure; D003461:Crystallography; D011755:Pyrophosphatases / Q000302:isolation & purification* / Q000648:ultrastructure; D016963:Thermus thermophilus / Q000201:enzymology*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D011755:Pyrophosphatases