1GVF

Structure of tagatose-1,6-bisphosphate aldolase

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Detector	MAR, RAXIS
Wavelength(s)	1.282,1.283,1.127,1.030, 1.5418,0.933
Spacegroup name	I 2 2 2
Unit cell lengths	72.650, 100.460, 206.660
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.450
R-factor	0.17 *
R-free	0.13000 *
Structure solution method	DIRECT METHODS
RMSD bond length	0.018
RMSD bond angle	0.030 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	RSPS
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.800	1.480
High resolution limit [Å]	1.450	1.450
Rmerge	0.064	0.292
Total number of observations	1086028 *
Number of reflections	131455 *
<I/σ(I)>	15	1.5
Completeness [%]	98.4	97.9
Redundancy	3	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	20 *	pH 6.40

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	6.5 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)	pH7.5
3	1	drop	PGH	20 (mM)
4	1	reservoir	ethylene glycol	7-12 (%(v/v))
5	1	reservoir		10 (mM)
6	1	reservoir	sodium cacodylate	42 (mM)	pH6.4