2HRA
Crystal structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA aminoacylation and nuclear export cofactor Arc1p reveal a novel function for an old fold
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-12-17 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97925 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 51.959, 107.113, 167.865 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 80.000 - 1.900 |
| R-factor | 0.21643 |
| Rwork | 0.214 |
| R-free | 0.26202 |
| Structure solution method | MAD |
| Starting model (for MR) | none |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.469 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | SHELXCD |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 80.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 37390 | |
| <I/σ(I)> | 13.2 | 4.2 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 4.7 | 4.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 1.8-1.9 M (NH4)2SO4, 200 mM NaI, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 1.8-1.9 M (NH4)2SO4, 200 mM NaI, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 1.8-1.9 M (NH4)2SO4, 200 mM NaI, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |






