2GHJ
Crystal structure of folded and partially unfolded forms of Aquifex aeolicus ribosomal protein L20
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 200 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-03-24 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 0.97961 |
| Spacegroup name | P 1 |
| Unit cell lengths | 44.914, 45.217, 67.060 |
| Unit cell angles | 104.06, 106.20, 97.76 |
Refinement procedure
| Resolution | 30.000 - 2.900 |
| R-factor | 0.22 |
| Rwork | 0.220 |
| R-free | 0.29200 |
| Structure solution method | SAD |
| Data reduction software | MOSFLM |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 30.000 |
| High resolution limit [Å] | 2.530 |
| Rmerge | 0.064 |
| Number of reflections | 21490 |
| <I/σ(I)> | 10.6 |
| Completeness [%] | 96.2 |
| Redundancy | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 294 | 50 mM Tris pH 7; 200 mM ammonium sulfate; 25 % PEG monomethyl ether, VAPOR DIFFUSION, HANGING DROP, temperature 294K |
