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

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

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: http://dx.doi.org/10.2174/0929866033478735

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

Publication date: 2003-10-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.