3RF2
Crystal Structure of 30S Ribosomal Protein S8 from Aquifex Aeolicus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL11-1 |
| Synchrotron site | SSRL |
| Beamline | BL11-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-06-23 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 96.235, 96.235, 37.614 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.432 - 2.160 |
| R-factor | 0.2275 |
| Rwork | 0.223 |
| R-free | 0.26740 |
| Structure solution method | MAD, MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.987 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.2.4) |
| Refinement software | PHENIX (1.7_650) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.240 |
| High resolution limit [Å] | 2.160 | 4.650 | 2.160 |
| Rmerge | 0.062 | 0.043 | 0.236 |
| Number of reflections | 9918 | ||
| <I/σ(I)> | 14.4 | ||
| Completeness [%] | 99.3 | 99.4 | 96.1 |
| Redundancy | 12.3 | 13.4 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 4.6 | 295 | 40% PEG 400, 0.1M sodium acetate, 0.2M lithium sulphate, pH 4.6, VAPOR DIFFUSION, temperature 295K |
| 1 | VAPOR DIFFUSION | 4.6 | 295 | 40% PEG 400, 0.1M sodium acetate, 0.2M lithium sulphate, pH 4.6, VAPOR DIFFUSION, temperature 295K |






