1P0M

Crystal structure of human butyryl cholinesterase in complex with a choline molecule

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
Collection date	2002-02-24
Detector	MARRESEARCH
Wavelength(s)	0.9798
Spacegroup name	I 4 2 2
Unit cell lengths	154.657, 154.657, 128.570
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.430 - 2.320 *
R-factor	0.215
Rwork	0.215
R-free	0.24400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1p0i
RMSD bond length	0.008
RMSD bond angle	23.400 *
Data scaling software	XDS
Phasing software	CNS
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.430	2.470
High resolution limit [Å]	2.320	2.320
Rmerge	0.061 *	0.398 *
Number of reflections	29378
<I/σ(I)>	23.67	4.26
Completeness [%]	87.4	77.7
Redundancy	9.9	6.7

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)