1A4O
14-3-3 PROTEIN ZETA ISOFORM
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Collection date | 1995-02 |
Spacegroup name | P 65 |
Unit cell lengths | 94.900, 94.900, 236.700 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.800 |
R-factor | 0.31 |
Rwork | 0.310 |
R-free | 0.34500 |
Structure solution method | MIRAS |
RMSD bond length | 0.010 |
RMSD bond angle | 1.840 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 10.000 |
High resolution limit [Å] | 2.800 |
Rmerge | 0.074 * |
Number of reflections | 28237 |
<I/σ(I)> | 11.6 |
Completeness [%] | 96.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | 4 * | pH 8.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5-10 (mg/ml) | |
2 | 1 | reservoir | PEG3500 | 20-24 (%) | |
3 | 1 | reservoir | Tris-HCl | 100 (mM) | pH8.5 |
4 | 1 | reservoir | 10 (mM) | ||
5 | 1 | reservoir | 1 (mM) |