Initiating a crystallographic study of a class II fructose-1,6-bisphosphate aldolase.
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.
Naismith
J H
JH
Department of Chemistry, University of Manchester, U.K.
Ferrara
J D
JD
Bailey
S
S
Marshall
K
K
Dauter
Z
Z
Wilson
K S
KS
Habash
J
J
Harrop
S J
SJ
Berry
A J
AJ
Hunter
W N
WN
D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology; D005634:Fructose-Bisphosphate Aldolase / Q000737:chemistry* / Q000302:isolation & purification; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D014961:X-Ray Diffraction / Q000379:methods
D007527:Isoenzymes; D005634:Fructose-Bisphosphate Aldolase