1E3M
The crystal structure of E. coli MutS binding to DNA with a G:T mismatch
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-02-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 89.960, 92.370, 261.330 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.200 |
| R-factor | 0.22891 * |
| Rwork | 0.228 |
| R-free | 0.26613 * |
| Structure solution method | MAD |
| RMSD bond length | 0.012 * |
| RMSD bond angle | 1.173 * |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SnB |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.065 | 0.469 |
| Number of reflections | 109670 | |
| <I/σ(I)> | 15.9 | 2.2 |
| Completeness [%] | 98.7 | 95.1 |
| Redundancy | 3.7 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | used microseeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 14 (mg/ml) | |
| 2 | 1 | drop | HEPES | 25 (mM) | |
| 3 | 1 | drop | 250 (mM) | ||
| 4 | 1 | drop | beta-mercaptoethanol | 10-20 (mM) | |
| 5 | 1 | reservoir | PEG6000 | 12-14 (%) | |
| 6 | 1 | reservoir | 150-300 (mM) | ||
| 7 | 1 | reservoir | HEPES | 100 (mM) | |
| 8 | 1 | reservoir | 10 (mM) | ||
| 9 | 1 | reservoir | ADP | 0.100-0.150 (mM) |
