1QFZ
PEA FNR Y308S MUTANT IN COMPLEX WITH NADPH
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1998-02-01 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 50.360, 110.090, 80.920 |
Unit cell angles | 90.00, 93.92, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.700 |
R-factor | 0.201 * |
Rwork | 0.201 |
R-free | 0.23500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Y308S:NADP+ |
RMSD bond length | 0.019 |
RMSD bond angle | 1.900 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.790 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.058 * | 0.334 * |
Total number of observations | 357117 * | |
Number of reflections | 92562 | |
<I/σ(I)> | 9 | 2.4 |
Completeness [%] | 96.1 | 90.6 |
Redundancy | 3.9 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 | 25 * | pH 8.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 4.5 (mg/ml) | |
2 | 1 | drop | potassium phosphate | 5 (mM) | |
3 | 1 | reservoir | ammonium sulfate | 2.1 (M) | |
4 | 1 | reservoir | Tris-HCl | 0.1 (M) |