3RBN
Crystal structure of MutL protein homolog 1 isoform 1 [Homo sapiens]
Experimental procedure
| Experimental method | SAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-03-25 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 63.505, 64.700, 130.932 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.582 - 2.160 |
| R-factor | 0.20933 |
| Rwork | 0.208 |
| R-free | 0.25123 |
| Structure solution method | SAD |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.272 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.582 | 2.200 |
| High resolution limit [Å] | 2.160 | 2.160 |
| Rmerge | 0.097 | 0.628 |
| Number of reflections | 29752 | |
| <I/σ(I)> | 25.5 | 2 |
| Completeness [%] | 100.0 | 99.9 |
| Redundancy | 8.7 | 6.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 22% PEG4000, 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
