3SR2
Crystal Structure of Human XLF-XRCC4 Complex
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] | 90 |
Detector technology | CCD |
Collection date | 2011-03-01 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.116 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 110.017, 110.017, 763.680 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 67.436 - 3.971 |
R-factor | 0.3586 |
Rwork | 0.358 |
R-free | 0.36900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2r9a |
RMSD bond length | 0.018 |
RMSD bond angle | 1.256 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.6.1_357) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 70.000 | 70.000 | 3.970 |
High resolution limit [Å] | 3.900 | 10.570 | 3.900 |
Rmerge | 0.131 | 0.067 | |
Number of reflections | 26221 | ||
<I/σ(I)> | 2.6 | ||
Completeness [%] | 98.8 | 94 | 88.7 |
Redundancy | 23.8 | 18.6 | 21.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7 | 303.15 | protein combined with equal volumes of 100 mM HEPES, pH 7.8, 13% (w/v) PEG 3350, 300 mM NaCl, 2 mM ADP, 7 mM NaF and 3 mM BeCl) and then dehydrated over 1000 ul of 19% PEG 3350, 300 mM NaCl, 100 mM HEPES, pH7.8 under argon., vapor diffusion, temperature 303.15K |