4PN7
Crystal Structure of the TFIIH p34 N-terminal Domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-12-01 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.91985 |
Spacegroup name | F 41 3 2 |
Unit cell lengths | 257.110, 257.110, 257.110 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 77.522 - 2.801 |
R-factor | 0.2197 |
Rwork | 0.219 |
R-free | 0.23800 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.783 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA (3.3.21) |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 148.443 | 77.522 | 2.950 |
High resolution limit [Å] | 2.801 | 8.850 | 2.800 |
Rmerge | 0.064 | 2.598 | |
Rmeas | 0.155 | ||
Rpim | 0.019 | 0.010 | 0.297 |
Total number of observations | 1305233 | 34950 | 201698 |
Number of reflections | 18512 | ||
<I/σ(I)> | 20.9 | 38.1 | 2.9 |
Completeness [%] | 100.0 | 99.9 | 100 |
Redundancy | 70.5 | 49.6 | 76.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | Crystals grew from protein solution in 20 mM Tris-HCl pH 8.0, 150 mM KCl and 1 mM TCEP over a reservoir containing the protein buffer including 50 - 500 mM NaCl |