5C7F
Crystal structure of the rice Topless related protein 2 (TPR2) N-terminal domain (1-209) in complex with Arabidopsis IAA1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-02-07 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9787 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 58.509, 129.284, 79.171 |
| Unit cell angles | 90.00, 110.11, 90.00 |
Refinement procedure
| Resolution | 41.863 - 2.700 |
| R-factor | 0.2243 |
| Rwork | 0.223 |
| R-free | 0.25620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4zhe |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.299 |
| 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 | 2.850 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.072 | 0.678 |
| Number of reflections | 30324 | |
| <I/σ(I)> | 15 | 2 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 5.2 | 4.3 |
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 |
