6CZM
Crystal structure of Medicago truncatula ATP-phosphoribosyltransferase in tense form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-08-10 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 89.170, 178.660, 92.110 |
| Unit cell angles | 90.00, 105.71, 90.00 |
Refinement procedure
| Resolution | 43.295 - 2.880 |
| R-factor | 0.192 |
| Rwork | 0.191 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Domains of MedtrATP-PRT1 in relaxed form |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.033 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.950 |
| High resolution limit [Å] | 2.880 | 2.880 |
| Rmerge | 0.047 | 0.800 |
| Rmeas | 0.055 | 0.930 |
| Number of reflections | 62118 | 4580 |
| <I/σ(I)> | 18.4 | 1.8 |
| Completeness [%] | 99.1 | 99.5 |
| Redundancy | 3.8 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 292 | histidine and AMP (5 mM each) were added to the protein solution supplemented with 10 mM MgCl2 and 100 mM KCl and incubated for 1 h. Reservoir solution: 2.53 M NaCl, 100 mM Bis-Tris propane pH 6.3 and 10% glycerol |
