3DLU
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 | 2005-10-03 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | .92004 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 44.074, 79.699, 60.548 |
| Unit cell angles | 90.00, 107.65, 90.00 |
Refinement procedure
| Resolution | 42.000 - 1.800 |
| R-factor | 0.2247 |
| Rwork | 0.191 |
| R-free | 0.22470 |
| Structure solution method | SAD |
| Starting model (for MR) | experimental phasing |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.030 |
| 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 | 1.850 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.069 | 0.427 |
| Number of reflections | 37519 | |
| <I/σ(I)> | 14.9 | 2.7 |
| Completeness [%] | 99.8 | 98.3 |
| Redundancy | 4.1 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 273 | 1.2-1.3M Na Malonate, 100mM Na Acetate, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 273K |
