2FOK
STRUCTURE OF RESTRICTION ENDONUCLEASE FOKI
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 130 |
Detector technology | IMAGE PLATE |
Collection date | 1997-01-20 |
Detector | FUJI |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.010, 137.170, 188.870 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.300 |
R-factor | 0.211 |
Rwork | 0.211 |
R-free | 0.30600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fok |
RMSD bond length | 0.007 |
RMSD bond angle | 25.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.082 | 0.364 |
Number of reflections | 61150 | |
<I/σ(I)> | 21.3 | 4.4 |
Completeness [%] | 95.9 | 81.9 |
Redundancy | 13.4 | 4.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.5 | PROTEIN CRYSTALLIZED IN 22% PEG 8000, 0.4 M AMMONIUM SULFATE, 0.1 M SODIUM CACODYLATE, PH 6.5. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 0.12 (mM) | |
10 | 1 | drop | glycerol | 5 (%) | |
11 | 1 | reservoir | PEG8000 | 22 (%) | |
12 | 1 | reservoir | ammonium sulfate | 0.4 (M) | |
13 | 1 | reservoir | sodium cacodylate | 0.1 (M) | pH6.5 |
2 | 1 | drop | PEG8000 | 11 (%) | |
3 | 1 | drop | ammonium sulfate | 0.2 (M) | |
4 | 1 | drop | sodium cacodylate | 50 (mM) | pH6.5 |
5 | 1 | drop | 0.2 (M) | ||
6 | 1 | drop | potassium phosphate | 10 (mM) | |
7 | 1 | drop | dithiothreitol | 0.5 (mM) | |
8 | 1 | drop | EDTA | 0.5 (mM) | |
9 | 1 | drop | EGTA | 0.5 (mM) |