1IVN

E.coli Thioesterase I/Protease I/Lysophospholiase L1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL38B1
Synchrotron site	SPring-8
Beamline	BL38B1
Temperature [K]	133
Detector technology	CCD
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9236
Spacegroup name	P 43 21 2
Unit cell lengths	49.936, 49.936, 170.364
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.100 * - 1.900
Rwork	0.229
R-free	0.25200 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1jrl
RMSD bond length	0.006
RMSD bond angle	1.200 *
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	28.100 *	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.046	0.246
Number of reflections	17893 *
<I/σ(I)>	12.9	4.94
Completeness [%]	97.0	87.2
Redundancy	21.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7 *	298	2-[N-morpholino]ethanesulfonic acid, PEGMME 5000, 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))