6UR7
Crystal structure of Sel1 repeat protein from Oxalobacter formigenes
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-12-17 |
| Detector | DECTRIS PILATUS3 X 6M |
| Wavelength(s) | 0.97985 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 78.824, 78.824, 210.242 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.730 - 2.709 |
| R-factor | 0.2214 |
| Rwork | 0.219 |
| R-free | 0.26980 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | low resolution SAD model |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.760 |
| High resolution limit [Å] | 2.709 | 7.350 | 2.709 |
| Rmerge | 0.157 | 0.076 | 0.916 |
| Rmeas | 0.165 | 0.080 | 1.009 |
| Rpim | 0.050 | 0.025 | 0.411 |
| Number of reflections | 18880 | 1093 | 895 |
| <I/σ(I)> | 6.8 | ||
| Completeness [%] | 99.9 | 99.6 | 99.7 |
| Redundancy | 10.6 | 10.7 | 5.6 |
| CC(1/2) | 0.988 | 0.690 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 289 | 0.2M Lithium sulfate, 0.1M Tris-Cl, 40% PEG400 |






