1WBD
Crystal structure of E. coli DNA mismatch repair enzyme MutS, E38Q mutant, in complex with a G.T mismatch
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-04-20 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 89.620, 92.042, 260.977 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.400 |
| R-factor | 0.213 |
| Rwork | 0.212 |
| R-free | 0.25900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1e3m |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.452 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.120 | 0.690 |
| Number of reflections | 85073 | |
| <I/σ(I)> | 11.9 | 1.78 |
| Completeness [%] | 99.3 | 92.9 |
| Redundancy | 6.72 | 5.75 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 25 MM HEPES(7.5), 300 MM NACL, 10 MM MGCL2, 14 % PEG 6000., pH 7.50 |
