4CZ5
Truncated tetramerization domain of zebrafish p53 (crystal form I)
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 21 21 21 |
Unit cell lengths | 33.232, 33.685, 101.805 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 28.100 - 1.020 |
R-factor | 0.15866 |
Rwork | 0.158 |
R-free | 0.17846 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.339 |
Refinement software | REFMAC (5.8.0069) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.090 | 1.080 |
High resolution limit [Å] | 1.020 | 1.020 |
Rmerge | 0.030 | 0.540 |
Number of reflections | 59076 | |
<I/σ(I)> | 19.3 | 3 |
Completeness [%] | 99.8 | 99.9 |
Redundancy | 5.2 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293 | SITTING DROP VAPOR DIFFUSION AT 20 DEGREE C; PROTEIN SOLUTION: 17 MG/ML IN 20 MM TRIS PH 7.5, 50 MM NACL, 5 MM DTT; CRYSTALLIZATION BUFFER: 2.4 M AMMONIUM SULFATE, 100 MM BICINE, PH 9.0 |