PMID:1613797
| Citation |
Naismith, JH, Ferrara, JD, Bailey, S, Marshall, K, Dauter, Z, Wilson, KS, Habash, J, Harrop, SJ, Berry, AJ and Hunter, WN (1992) Initiating a crystallographic study of a class II fructose-1,6-bisphosphate aldolase. J. Mol. Biol. 225:1137-41 |
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| Abstract |
We have reproducibly crystallized the metal-dependent Class II fructose-1,6-bisphosphate aldolase from Escherichia coli. Crystals in the shape of truncated hexagonal bipyramids have unit cell dimensions of a = b = 78.4 A, c = 290.6 A and are suitable for a detailed structural analysis. The space group has been identified as P6(1)22 or enantiomorph. Data sets to approximately 2.9 A resolution have been recorded using both the Rigaku R-AXIS IIc image plate area detector coupled to a copper target rotating anode X-ray source and using the MAR image plate systems with synchrotron radiation at the EMBL outstation DESY in Hamburg, and at S.R.S. Daresbury. Diffraction beyond 2.5 A has been observed when large freshly grown crystals are used with the synchrotron beam. A data set to this resolution has been collected. Several putative heavy-atom derivative data sets have also been measured using synchrotron radiation facilities and analysis of these data sets is in progress. |
| Links | |
| Keywords |
Crystallization; Escherichia coli/enzymology; Fructose-Bisphosphate Aldolase/chemistry; Fructose-Bisphosphate Aldolase/isolation & purification; Isoenzymes/chemistry; Isoenzymes/isolation & purification; Protein Conformation; X-Ray Diffraction/methods |
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