3FZ3
Crystal Structure of almond Pru1 protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 110 |
| Detector technology | IMAGE PLATE |
| Collection date | 2007-03-07 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 41 |
| Unit cell lengths | 151.021, 151.021, 165.367 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.080 - 2.400 |
| R-factor | 0.174 |
| Rwork | 0.172 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.015 |
| RMSD bond angle | 2.001 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 36.080 | 50.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 5.170 | 2.400 |
| Rmerge | 0.129 | 0.072 | 0.608 |
| Number of reflections | 142516 | ||
| <I/σ(I)> | 7.779 | ||
| Completeness [%] | 99.2 | 99.3 | 97.7 |
| Redundancy | 5.8 | 7 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 295 | 0.1 M Tris Hydrochloride pH 8.5, 2M Ammonium Sulfate, vapor diffusion, hanging drop, temperature 295K |
