2P6V
Structure of TAFH domain of the human TAF4 subunit of TFIID
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-03-16 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.9797, 1.0199 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 74.852, 74.852, 131.785 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 65.940 - 2.000 |
R-factor | 0.21567 |
Rwork | 0.214 |
R-free | 0.24835 |
Structure solution method | MAD |
RMSD bond length | 0.017 |
RMSD bond angle | 2.343 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | MLPHARE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 65.940 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.095 | 0.105 |
Number of reflections | 15423 | |
<I/σ(I)> | 16.7 | 3.7 |
Completeness [%] | 98.5 | 98.3 |
Redundancy | 13.9 | 10.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.6 | 295 | Crystals of methylated hTAF4-TAFH containing SeMet were grown by hanging drop vapor diffusion at 22 C by mixing equal volumes of protein solution and crystallization buffer (200 mM ammonium acetate, 2.2 M ammonium sulfate and 150 mM sodium bromide). , pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K |