8BTT
Structure of human RTCB
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-06-23 |
Detector | DECTRIS PILATUS3 X 6M |
Wavelength(s) | 1.0332 |
Spacegroup name | I 4 |
Unit cell lengths | 215.640, 215.640, 46.870 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.220 - 2.600 |
R-factor | 0.202 |
Rwork | 0.199 |
R-free | 0.25560 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Alphafold model for Q9Y3I0 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.517 |
Data reduction software | XDS (20210205) |
Data scaling software | Aimless (1.12.10) |
Phasing software | PHASER (2.8.3) |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.220 | 2.720 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.184 | |
Rpim | 0.077 | 0.875 |
Number of reflections | 33777 | 4030 |
<I/σ(I)> | 8.5 | 0.9 |
Completeness [%] | 100.0 | |
Redundancy | 6.7 | |
CC(1/2) | 0.995 | 0.348 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293.15 | protein: 125 uM in 25 mM Tris pH 7.5, 200 mM NaCl, 10 % glycerol, 1mM TCEP, 2 mM manganese chloride reservoir: 0.1 M magnesium chloride, 0.1 M HEPES pH 7.0, 15 % PEG 4000 drop: 800 nl protein + 600 nl reservoir |