1YRG
THE CRYSTAL STRUCTURE OF RNA1P: A NEW FOLD FOR A GTPASE-ACTIVATING PROTEIN
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-07-15 |
| Detector | MARRESEARCH |
| Spacegroup name | I 41 |
| Unit cell lengths | 175.530, 175.530, 55.800 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.660 |
| R-factor | 0.228 * |
| Rwork | 0.228 |
| R-free | 0.27700 |
| Structure solution method | MIRAS |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (0.4) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.690 |
| High resolution limit [Å] | 2.640 | 2.640 |
| Rmerge | 0.084 * | 0.196 * |
| Number of reflections | 24708 | |
| <I/σ(I)> | 18.2 | 4.2 |
| Completeness [%] | 97.8 | 58.9 |
| Redundancy | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 20 * | HANGING DROPS MADE FROM 2-4 MICROLITER OF PROTEIN SOLUTION (25 MG/ML RNA1P IN 0.02 M TRIS-HCL, 0.002 M DTE, PH 7.5) AND THE SAME VOLUME OF RESERVOIR SOLUTION (21-24% PEG 2000 MME, 0.1 M TRIS-HCL, 0.2 M LI2SO4, 0.02 M MGCL2, PH 8.5), VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG2000 MME | 21-24 (%) | |
| 2 | 1 | reservoir | Tris-HCl | 100 (mM) | |
| 3 | 1 | reservoir | 200 (mM) | ||
| 4 | 1 | reservoir | 20 (mM) | ||
| 5 | 1 | drop | protain | 25 (mg/ml) | |
| 6 | 1 | drop | Tris-HCl | 20 (mM) | |
| 7 | 1 | drop | DTE | 2 (mM) |
