Crystallization and preliminary X-ray analysis of fructose 6-phosphate, 2- kinase

Fructose 2,6-bisphosphatase

E. S. Istvan, C. A. Hasemann, R. G. Kurumbail, K. Uyeda, J. Deisenhofer

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Diffraction-quality crystals of the bifunctional enzyme fructose 6- phosphate, 2-kinase:fructose 2,6-bisphosphatase from rat testis have been obtained. The crystals were grown in the presence of ATPγS, fructose 6- phosphate, the detergent n-octylglucoside, and the precipitant polyethylene glycol 4000. The crystals have the symmetry of the trigonal space group P3( 1/2 )21 with a = b = 83.0 Å and c = 130.6 Å. Flash-frozen crystals diffract to beyond 2.2 Å, and native data have been collected.

Original languageEnglish (US)
Pages (from-to)2439-2441
Number of pages3
JournalProtein Science
Volume4
Issue number11
StatePublished - 1995

Fingerprint

Phosphofructokinase-2
X ray analysis
Crystallization
Detergents
Testis
X-Rays
Crystals
Enzymes
Crystal symmetry
Rats
Diffraction
fructose-6-phosphate
polyethylene glycol 4000
octyl-beta-D-glucoside

Keywords

  • bifunctional enzyme
  • enzyme mechanism
  • kinase
  • phosphatase glycolysis regulation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Crystallization and preliminary X-ray analysis of fructose 6-phosphate, 2- kinase : Fructose 2,6-bisphosphatase. / Istvan, E. S.; Hasemann, C. A.; Kurumbail, R. G.; Uyeda, K.; Deisenhofer, J.

In: Protein Science, Vol. 4, No. 11, 1995, p. 2439-2441.

Research output: Contribution to journalArticle

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AU - Kurumbail, R. G.

AU - Uyeda, K.

AU - Deisenhofer, J.

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KW - phosphatase glycolysis regulation

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