5J39
Crystal Structure of the extended TUDOR domain from TDRD2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-01-29 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97957 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 36.692, 53.798, 108.063 |
Unit cell angles | 90.00, 84.26, 90.00 |
Refinement procedure
Resolution | 34.110 - 1.950 |
R-factor | 0.1922 |
Rwork | 0.190 |
R-free | 0.22220 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3fdr |
RMSD bond length | 0.010 |
RMSD bond angle | 1.110 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.23) |
Phasing software | PHASER |
Refinement software | BUSTER-TNT (2.10.2) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 53.800 | 53.800 | 2.000 |
High resolution limit [Å] | 1.950 | 8.940 | 1.950 |
Rmerge | 0.087 | 0.020 | 1.114 |
Rmeas | 0.101 | 0.023 | 1.296 |
Rpim | 0.052 | 0.012 | 0.660 |
Total number of observations | 115581 | 1173 | 8066 |
Number of reflections | 30647 | ||
<I/σ(I)> | 12 | 42.7 | 1.6 |
Completeness [%] | 99.6 | 98.9 | 99 |
Redundancy | 3.8 | 3.4 | 3.8 |
CC(1/2) | 0.998 | 0.999 | 0.601 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 291 | 15% PEG-8000, 0.2 M magnesium chloride, 0.1 sodium cacodylate. A putative peptide ligand was added to the protein but not found during crystal structure analysis. |