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 |
