1QZ3

CRYSTAL STRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 COMPLEXED WITH HEXADECANESULFONATE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X13
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X13
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-02-15
Detector	MARRESEARCH
Wavelength(s)	0.8015
Spacegroup name	P 41 21 2
Unit cell lengths	85.193, 85.193, 103.585
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.300
R-factor	0.188
Rwork	0.174
R-free	0.21600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1evq
RMSD bond length	0.008
RMSD bond angle	1.530
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.340
High resolution limit [Å]	2.300	2.300
Rmerge	0.089 *	0.426 *
Total number of observations	177515 *
Number of reflections	17707
<I/σ(I)>	14.4	2.2
Completeness [%]	98.8	94.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	25 *	AMMONIUM SULPHATE, TRIS BUFFER, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	2 (M)
2	1	reservoir	Tris	0.1 (M)	pH8.5
3	1	drop	phosphate	20 (mM)
4	1	drop	acetonitrile	4 (%(v/v))
5	1	drop	enzyme	0.015 (mg/ml)