1C8U

CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF THE HUMAN NEF-BINDING ENZYME

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1997-11-10
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	95.902, 119.805, 165.479
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.900
R-factor	0.2303
Rwork	0.218
R-free	0.24800 *
RMSD bond length	0.005
RMSD bond angle	1.330
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.970
High resolution limit [Å]	1.900	1.900
Rmerge	0.059	0.425
Total number of observations	353158 *
Number of reflections	74901 *
<I/σ(I)>	10.8
Completeness [%]	99.7 *	99.4
Redundancy	4.7	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5 *	293	NACL, NAOAC, LDAO, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)
3	1	reservoir		2 (M)
4	1	reservoir		100 (mM)
5	1	reservoir	LDAO	5 (mM)