1EZJ
CRYSTAL STRUCTURE OF THE MULTIMERIZATION DOMAIN OF THE PHOSPHOPROTEIN FROM SENDAI VIRUS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-05-05 |
Detector | MARRESEARCH |
Spacegroup name | P 4 21 2 |
Unit cell lengths | 48.584, 48.584, 100.847 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.900 |
R-factor | 0.255 |
Rwork | 0.249 |
R-free | 0.29300 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.210 |
Data reduction software | DENZO |
Data scaling software | CCP4 ((TRUNCATE)) |
Phasing software | SHARP |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.089 | 0.386 |
Number of reflections | 9175 | |
<I/σ(I)> | 15 | |
Completeness [%] | 92.1 | 94.5 |
Redundancy | 3.7 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 20 * | PEG 3000 16%, Sodium chloride 200 mM, Calcium chloride 10 mM, ethylmercurythiosalicilic acid 5 mM, Tris-HCl 100 mM, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8 (mg/ml) | |
2 | 1 | drop | HEPES | 20 (mM) | |
3 | 1 | drop | 50 (mM) | ||
4 | 1 | reservoir | Tris-HCl | 100 (mM) | |
5 | 1 | reservoir | 200 (mM) | ||
6 | 1 | reservoir | 10 (mM) | ||
7 | 1 | reservoir | PEG3000 | 15-17 (%(w/v)) | |
8 | 1 | reservoir | EMTS | 5 (mM) |