1J00

E. coli Thioesterase I/Protease I/Lysophospholipase L1 in complexed with diethyl phosphono moiety

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSRRC BEAMLINE BL17B2
Synchrotron site	NSRRC
Beamline	BL17B2
Temperature [K]	133
Detector technology	IMAGE PLATE
Detector	MAC Science DIP-2030
Wavelength(s)	1.12714
Spacegroup name	P 43 21 2
Unit cell lengths	49.907, 49.907, 171.898
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 * - 2.000
Rwork	0.239
R-free	0.26700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1jrl
RMSD bond length	0.007 *
RMSD bond angle	1.200 *
Data reduction software	XPRESS
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.060 *	0.381
Number of reflections	15230 *
<I/σ(I)>	11.3	5.2
Completeness [%]	97.7 *	98.9
Redundancy	13.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7 *	298	2-[N-morpholino]ethanesulfonic acid, PEGMME5000, Ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	24.5 (mg/ml)
2	1	2	sodium phosphate	10 (mM)	pH7.0
3	1	2	PEG5000 MME	25.5 (%(w/w))