5GK8

Structure of E.Coli fructose 1,6-bisphosphate aldolase, Acetate bound form

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	PAL/PLS BEAMLINE 5C (4A)
Synchrotron site	PAL/PLS
Beamline	5C (4A)
Temperature [K]	100
Detector technology	CCD
Collection date	2014-07-10
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.979
Spacegroup name	P 1 21 1
Unit cell lengths	66.598, 73.351, 78.269
Unit cell angles	90.00, 102.63, 90.00

Refinement procedure

Resolution	36.605 - 2.002
R-factor	0.1622
Rwork	0.161
R-free	0.19980
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dos
Data reduction software	HKL-2000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	PHENIX ((1.10.1_2155: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.050
High resolution limit [Å]	2.000	2.000
Rmerge	0.091	0.359
Number of reflections	49638
<I/σ(I)>	40.2	7.6
Completeness [%]	100.0	100
Redundancy	6.3	6.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	287	0.2 M ammonium acetate, 5% fructose 1,6-bisphosphatase, 0.1 M Tris pH 7.0, and 15% PEG 4000