5TNU
S. tokodaii XPB II crystal structure at 3.0 Angstrom resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 12.3.1 |
Synchrotron site | ALS |
Beamline | 12.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-02-22 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 160.922, 160.922, 122.960 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.880 - 3.050 |
R-factor | 0.1976 |
Rwork | 0.196 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2fwr |
RMSD bond length | 0.010 |
RMSD bond angle | 1.312 |
Data reduction software | MOSFLM (7.2.0) |
Data scaling software | Aimless (0.5.12) |
Phasing software | PHASER (2.5.7) |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 29.880 | 29.880 | 3.210 |
High resolution limit [Å] | 3.050 | 9.640 | 3.050 |
Rmerge | 0.374 | 0.065 | 2.904 |
Rmeas | 0.382 | 0.066 | 2.967 |
Rpim | 0.078 | 0.014 | 0.609 |
Total number of observations | 740378 | 24703 | 105244 |
Number of reflections | 31341 | 1080 | 4504 |
<I/σ(I)> | 11.2 | 33.8 | 2 |
Completeness [%] | 99.9 | 96.7 | 100 |
Redundancy | 23.6 | 22.9 | 23.4 |
CC(1/2) | 0.996 | 0.999 | 0.629 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | 1:1 ratio of protein with 10 mM sodium citrate pH 5.6, 1770 mM ammonium sulfate |