1J1L
Crystal structure of human Pirin: a Bcl-3 and Nuclear factor I interacting protein and a cupin superfamily member
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44B2 |
Synchrotron site | SPring-8 |
Beamline | BL44B2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-11-01 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 0.9795, 0.9799, 0.9817 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 42.278, 67.116, 106.389 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.100 |
Rwork | 0.206 |
R-free | 0.24900 * |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.350 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.050 | 0.293 |
Total number of observations | 94836 * | |
Number of reflections | 30894 | |
<I/σ(I)> | 6.8 | 1.8 |
Completeness [%] | 89.9 | 79.8 |
Redundancy | 3.08 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 16 * | PEG 4000, 0.1M MES, 0.2M (NH4)2SO4, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25 (mg/ml) | |
2 | 1 | reservoir | PEG20000 | 14 (%) | |
3 | 1 | reservoir | MES | 0.1 (M) | pH6.5 |