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1J06

Crystal structure of mouse acetylcholinesterase in the apo form

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-4
Synchrotron siteESRF
BeamlineID14-4
Temperature [K]100
Detector technologyCCD
DetectorADSC QUANTUM 4
Wavelength(s)0.946
Spacegroup nameP 21 21 21
Unit cell lengths79.196, 111.974, 226.834
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution20.000 - 2.350
Rwork0.209
R-free0.23200
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1maa
RMSD bond length0.013
RMSD bond angle24.200

*

Data reduction softwareDENZO
Data scaling softwareSCALA
Phasing softwareAMoRE
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.000

*

High resolution limit [Å]2.350
Rmerge0.058

*

0.370

*

Total number of observations903557

*

Number of reflections83956
<I/σ(I)>9.5
Completeness [%]99.299.6

*

Redundancy5.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP4

*

PEG 600, HEPES OR SODIUM ACETATE, pH 6.5-8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein10-12 (mg/ml)
21reservoirPEG60025-32 (%(v/v))
31reservoirHEPES20-100 (mM)pH6.5-8.0

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PDB entries from 2025-07-30

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