1WBB
Crystal structure of E. coli DNA mismatch repair enzyme MutS, E38A mutant, in complex with a G.T mismatch
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-11-24 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 89.553, 92.494, 261.264 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.500 |
| R-factor | 0.221 |
| Rwork | 0.220 |
| R-free | 0.27000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1e3m |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.225 |
| 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 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.110 | 0.720 |
| Number of reflections | 75289 | |
| <I/σ(I)> | 9.81 | 1.48 |
| Completeness [%] | 99.3 | 98.3 |
| Redundancy | 3.12 | 3.06 |
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 |
