1OHA

Acetylglutamate kinase from Escherichia coli complexed with MgADP and N-acetyl-L-glutamate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-2
Synchrotron site	ESRF
Beamline	ID14-2
Temperature [K]	100
Detector technology	CCD
Collection date	2000-05-10
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	60.126, 71.792, 107.175
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.430 - 1.900
R-factor	0.2
Rwork	0.200
R-free	0.22950
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gs5
RMSD bond length	0.005
RMSD bond angle	1.500
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.430	2.000
High resolution limit [Å]	1.900	1.900
Rmerge	0.068	0.469
Total number of observations	154986 *
Number of reflections	18636
<I/σ(I)>	7.3	1.3
Completeness [%]	99.9	99.6
Redundancy	8.3	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	4.6		27-29% POLYETHYLENE GLYCOL MONOMETHYL ETHER 2K, SODIUM ACETATE 0.1M PH 4.6 AMMONIUM SULFATE 0.15-0.3 M

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG2000	27-29 (%(w/v))
2	1	reservoir	sodium acetate	0.1 (M)	pH4.6
3	1	reservoir	ammonium citrate	0.25-0.4 (M)
4	1	drop	protein	10 (mg/ml)