3DM5
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 | 2005-06-03 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.11589 |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 127.009, 127.009, 186.836 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 64.740 - 2.510 |
| R-factor | 0.223 |
| Rwork | 0.222 |
| R-free | 0.25900 |
| Structure solution method | SAD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.168 |
| 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] | 64.740 | 2.560 |
| High resolution limit [Å] | 2.510 | 2.510 |
| Rmerge | 0.056 | 0.763 |
| Number of reflections | 53350 | |
| <I/σ(I)> | 12.7 | 1.7 |
| Completeness [%] | 99.5 | 98.4 |
| Redundancy | 4.1 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 1.0-1.3M Lithium Sulfate, 100mM Na Acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
