3DLV
Structures of SRP54 and SRP19, the two proteins assembling the ribonucleic core of the Signal Recognition Particle from the archaeon Pyrococcus furiosus.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2006-05-08 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.97949 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 35.316, 116.052, 84.460 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.800 - 1.870 |
| R-factor | 0.205 |
| Rwork | 0.199 |
| R-free | 0.25800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3dul |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.812 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.940 |
| High resolution limit [Å] | 1.870 | 1.870 |
| Rmerge | 0.052 | 0.513 |
| Number of reflections | 14745 | |
| <I/σ(I)> | 22.3 | 2 |
| Completeness [%] | 100.0 | 98.3 |
| Redundancy | 7.9 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 1.2-1.3M Na Malonate, 100 mM NaAcetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
