1IGW

Crystal Structure of the Isocitrate Lyase from the A219C mutant of Escherichia coli

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1995-11-19
Detector	MARRESEARCH
Wavelength(s)	0.92
Spacegroup name	P 32
Unit cell lengths	88.650, 88.650, 199.400
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	15.000 - 2.100
R-factor	0.184 *
Rwork	0.184
R-free	0.23500
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.600
Data reduction software	MOSFLM
Data scaling software	CCP4 ((AGROVATA)
Phasing software	CCP4
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.300	2.150
High resolution limit [Å]	2.100	2.100
Rmerge	0.051	0.216
Total number of observations	188246 *
Number of reflections	96329	6893 *
Completeness [%]	94.1	91.3
Redundancy	2	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	290	MEPEG 2000, magnesium chloride, ethyl mercury thiosalicylate, HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	HEPES	0.1 (M)
2	1	drop		5 (mM)
3	1	reservoir	mPEG2000	20-22 (%(w/v))
4	1	reservoir	EMTS	5 (mM)