2PM8
Crystal structure of recombinant full length human butyrylcholinesterase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2005-12-12 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 4 21 2 |
Unit cell lengths | 150.803, 150.803, 142.120 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.800 |
R-factor | 0.22516 |
Rwork | 0.222 |
R-free | 0.29221 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1xlw |
RMSD bond length | 0.012 |
RMSD bond angle | 1.536 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.250 | 2.950 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.129 | 0.545 |
Number of reflections | 38439 | |
<I/σ(I)> | 11.6 | 1.6 |
Completeness [%] | 95.0 | 82.4 |
Redundancy | 4.9 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | Ammonium sulphate, pH 8.5, VAPOR DIFFUSION, SITTING DROP |