2P5X
Crystal structure of Maf domain of human N-acetylserotonin O-methyltransferase-like protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-01-28 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 1.54000 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 84.802, 116.983, 51.471 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.070 - 2.000 |
R-factor | 0.20077 |
Rwork | 0.198 |
R-free | 0.25309 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ex2 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.429 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 25.070 |
High resolution limit [Å] | 2.000 |
Rmerge | 0.167 |
Number of reflections | 35334 |
<I/σ(I)> | 5.9 |
Completeness [%] | 99.7 |
Redundancy | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 300 | 15% PEG 3350, 0.1 M Succinic acid, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 300K |