4D1M
Tetramerization domain of zebrafish p53 (crystal form II)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I03 |
Synchrotron site | Diamond |
Beamline | I03 |
Temperature [K] | 100 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 70.861, 74.507, 74.945 |
Unit cell angles | 90.00, 117.79, 90.00 |
Refinement procedure
Resolution | 28.900 - 2.200 |
R-factor | 0.22845 |
Rwork | 0.226 |
R-free | 0.27996 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.336 |
Refinement software | REFMAC (5.8.0069) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.900 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.040 | 0.520 |
Number of reflections | 34925 | |
<I/σ(I)> | 14.8 | 2.5 |
Completeness [%] | 99.3 | 99.5 |
Redundancy | 3.4 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | SITTING DROP VAPOR DIFFUSION AT 20 DEGREE C; PROTEIN SOLUTION: 12 MG/ML IN 20 MM TRIS PH 7.5, 50 MM NACL, 5 MM DTT; CRYSTALLIZATION BUFFER: 160 MM ZINC ACETATE, 80 MM SODIUM CACODYLATE, PH 6.5, 12% (W/V) POLYETHYLENE GLYCOL 8,000 AND 19% (W/V) GLYCEROL |