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Crystallization and preliminary X-ray crystallographic analysis of recombinant transaldolase B from Eschericha coli.

Recombinant transaldolase from Escherichia coli, an enzyme of the pentose phosphate pathway has been crystallized by the vapor-diffusion method using polyethylene glycol 6000 as precipitant. The crystals are orthorhombic, space group P2(1)2(1)2(1) with cell dimensions a = 68.9, b = 91.3 and c = 130.5 A and diffract to 2 A resolution on a conventional X-ray source. The asymmetric unit very likely contains two subunits, corresponding to a packing density of 2.9 A(3) Da(-1).[1]

References

  1. Crystallization and preliminary X-ray crystallographic analysis of recombinant transaldolase B from Eschericha coli. Jia, J., Lindqvist, Y., Schneider, G., Schörken, U., Sahm, H., Sprenger, G.A. Acta Crystallogr. D Biol. Crystallogr. (1996) [Pubmed]
 
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