5C6V
Crystal structure of the rice Topless related protein 2 (TPR2) N-terminal domain (1-209) in complex with Arabidopsis NINJA peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-03-14 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.078 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 81.743, 65.042, 107.735 |
| Unit cell angles | 90.00, 105.40, 90.00 |
Refinement procedure
| Resolution | 48.495 - 3.100 |
| R-factor | 0.2349 |
| Rwork | 0.232 |
| R-free | 0.28640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4zhe |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.411 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.310 |
| High resolution limit [Å] | 3.100 | 3.100 |
| Rmerge | 0.172 | 0.566 |
| Number of reflections | 20063 | |
| <I/σ(I)> | 5.9 | 2.2 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 4.1 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 25% w/v PEG 3,350, 0.2 M NaCl, 0.1 M BIS-TRIS pH 5.5, 3.0% w/v D-(+)-glucose monohydrate |
