1GQS
ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH NAP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-08-15 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 111.040, 111.040, 137.227 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.200 - 3.000 |
R-factor | 0.212 |
Rwork | 0.212 |
R-free | 0.26200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ACE |
RMSD bond length | 0.008 |
RMSD bond angle | 23.000 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.200 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.160 | 0.529 * |
Total number of observations | 243327 * | |
Number of reflections | 20097 * | |
<I/σ(I)> | 5 | 1.4 |
Completeness [%] | 99.4 | 98.4 * |
Redundancy | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.8 | 4 * | pH 5.80 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG200 | 34-38 (%(v/v)) | |
2 | 1 | reservoir | MES | 0.1 (M) | pH5.8 |
3 | 1 | drop | protein | 11 (mg/ml) |