6LBK
Structure of rat GLD-2 (Terminal nucleotidyltransferase 2, TENT2)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-04-02 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.977760 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 79.960, 40.720, 105.000 |
Unit cell angles | 90.00, 100.20, 90.00 |
Refinement procedure
Resolution | 47.198 - 2.496 |
R-factor | 0.206856945188 |
Rwork | 0.205 |
R-free | 0.24253 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5jnb |
RMSD bond length | 0.010 |
RMSD bond angle | 1.213 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MrBUMP |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.200 | 2.580 |
High resolution limit [Å] | 2.490 | 2.496 |
Rmerge | 0.050 | 0.524 |
Number of reflections | 44966 | 23510 |
<I/σ(I)> | 21.5 | |
Completeness [%] | 99.1 | |
Redundancy | 6.5 | |
CC(1/2) | 0.999 | 0.914 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291.15 | 22.4% PEG 3350, 100 mM Tris-HCl pH 8.0 |