3K05
The crystal structure of MDC1 BRCT T2067D in complex with a minimal recognition tetrapeptide with an amidated C-terminus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-13 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.115872 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.642, 74.580, 103.408 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.950 - 1.330 |
| R-factor | 0.18298 |
| Rwork | 0.182 |
| R-free | 0.20211 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.306 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.1) |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.380 |
| High resolution limit [Å] | 1.330 | 2.870 | 1.330 |
| Rmerge | 0.050 | 0.036 | 0.489 |
| Number of reflections | 97906 | ||
| <I/σ(I)> | 16.9 | ||
| Completeness [%] | 98.3 | 98.1 | 95.7 |
| Redundancy | 3.8 | 3.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8 | 298 | PEG 8000, HEPES, pH 8.0, vapor diffusion, temperature 298K |
