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1VZJ

Structure of the tetramerization domain of acetylcholinesterase: four-fold interaction of a WWW motif with a left-handed polyproline helix

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X4A
Synchrotron siteNSLS
BeamlineX4A
Temperature [K]100
Collection date2001-04-15
Wavelength(s)0.96672,0.97927,0.97895,1.5415
Spacegroup nameP 1 21 1
Unit cell lengths53.730, 58.790, 58.800
Unit cell angles90.00, 111.38, 90.00
Refinement procedure
Resolution40.000 - 2.350
R-factor0.247
Rwork0.247
R-free0.25900
Structure solution methodMAD
RMSD bond length0.009
RMSD bond angle1.202
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSOLVE/RESOLVE
Refinement softwareCNS (1.1)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]29.0002.380
High resolution limit [Å]2.3002.300
Rmerge0.0540.349
Number of reflections12935
<I/σ(I)>11.11.47
Completeness [%]89.458.5
Redundancy2.71.75
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
15.610% ISOPROPANOL, 10% PEG, 4K 0.05 M TRISODIUM CITRATE, PH 5.6

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