7QBF
TC:CD320 in complex with nanobody TC-Nb34
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-03-11 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 104.822, 104.822, 167.460 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.270 - 1.850 |
R-factor | 0.1759 |
Rwork | 0.174 |
R-free | 0.20480 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4zrp |
RMSD bond length | 0.012 |
RMSD bond angle | 2.577 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.270 | 1.920 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.027 | |
Number of reflections | 158598 | 15319 |
<I/σ(I)> | 1.89 | |
Completeness [%] | 98.2 | |
Redundancy | 2 | |
CC(1/2) | 0.999 | 0.442 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293.15 | 200 mM Ammonium Iodide, 16% w/v PEG 3350 and 1.4 x 105-fold diluted seed stocks from crystals of the same protein, grown in similar conditions |