5ITQ
Crystal Structure of Human NEIL1, Free Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-08-01 |
Detector | MAR CCD 130 mm |
Wavelength(s) | 0.9793 |
Spacegroup name | H 3 |
Unit cell lengths | 132.454, 132.454, 50.791 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 66.230 - 1.480 |
R-factor | 0.158 |
Rwork | 0.156 |
R-free | 0.19600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tdh |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 66.230 | 1.530 |
High resolution limit [Å] | 1.480 | 1.480 |
Rmerge | 0.065 | 0.840 |
Number of reflections | 52396 | |
<I/σ(I)> | 27.27 | 2.63 |
Completeness [%] | 99.6 | 100 |
Redundancy | 5.6 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 6.5 | 277 | 0.1M cacodylic acid (pH 7.0), 0.1M NaCl, 0.05 M MgCl2, 24%(w/v) PEG 8000 |