1P0P

Crystal structure of soman-aged human butyryl cholinesterase in complex with the substrate analog butyrylthiocholine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Detector	MARRESEARCH
Wavelength(s)	0.933
Spacegroup name	I 4 2 2
Unit cell lengths	154.924, 154.924, 127.909
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	54.700 * - 2.300
R-factor	0.199
Rwork	0.199
R-free	0.24200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1p0i
RMSD bond length	0.006
RMSD bond angle	23.600 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	CNS
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	54.700 *	2.420
High resolution limit [Å]	2.300	2.300
Rmerge	0.081 *	0.264 *
Number of reflections	28730
<I/σ(I)>	8.1	2.8
Completeness [%]	86.5	49.6 *
Redundancy	6.4	5.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	20 *	Nachon, F., (2002) Eur.J.Biochem., 269, 630. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6.6 (mg/ml)
2	1	drop	MES	0.1 (M)	pH6.5
3	1	reservoir	ammonium sulfate	2.05-2.15 (M)