Crystallization And Preliminary X-Ray Analysis Of Class Ii Fructose-1,6-Bisphosphate Aldolase From Thermus Caldophilus

Authors: Lee J.H.¹; Im Y.J.u.n.¹; Rho S-H.¹; Park S.H.o.¹; Kim M-K.¹; Cho S.J.i.n.¹; Kim T-Y.¹; Oh J.H.w.a.n.¹; Shin H-J.¹; Lee D-S.¹; Eom S.H.y.u.n.¹

Source: Protein and Peptide Letters, Volume 10, Number 5, October 2003 , pp. 511-515(5)

Publisher: Bentham Science Publishers

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Abstract:

In this study, we have crystallized class II fructose-1,6-bisphosphate aldolase (FBA) from Thermus caldophilus (Tca). Purified Tca FBA is a tetrameric enzyme of 305 residues, which crystallizes in the space group P212121 (cell dimensions a = 98.9, b = 113.1, c = 115.7 Å), with four molecules in the asymmetric unit. A complete diffraction data set was obtained from orthorhombic crystals at resolution of 2.2 Å.

Keywords: fructose; bisphosphate aldolase; dihydroxyaceton phosphate; glyceraldehydes-3-phosphate; thermus caldophilus

Document Type: Review article

DOI: 10.2174/0929866033478735

Affiliations: 1: Department of Life Science, Kwangju Institute of Science & Technology, Gwangju 500-712, Korea

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