5C6Q
Crystal structure of the apo TOPLESS related protein 2 (TPR2) N-terminal domain (1-209) from rice
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 | 2014-10-30 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.27821 |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 58.971, 58.971, 171.743 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.710 - 3.251 |
R-factor | 0.2151 |
Rwork | 0.213 |
R-free | 0.26970 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4zhe |
RMSD bond length | 0.008 |
RMSD bond angle | 1.281 |
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 | 3.430 |
High resolution limit [Å] | 3.250 | 3.250 |
Number of reflections | 10544 | |
<I/σ(I)> | 27.5 | 3.5 |
Completeness [%] | 100.0 | 100 |
Redundancy | 15.3 | 15.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 25% PEG 3350, 0.2 M magnesium chloride, 0.1 M BIS-TRIS, pH 6.5 |