1MAA

MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATED PROTEIN

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-12
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	136.550, 173.130, 224.250
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.900
R-factor	0.2
Rwork	0.200
R-free	0.24800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1mah
RMSD bond length	0.011
RMSD bond angle	24.600 *
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.000
High resolution limit [Å]	2.900	2.900
Rmerge	0.105 *	0.370 *
Total number of observations	604052 *
Number of reflections	107379
<I/σ(I)>	7	2
Completeness [%]	92.0	83
Redundancy	2.8	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7	4 *	protein solution is mixed in a 1:1 ratio with well solution *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir		1.7 (M)
2	1	reservoir		10 (mM)