5T2S
Structure of the FHA1 domain of Rad53 bound simultaneously to the BRCT domain of Dbf4 and a phosphopeptide.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CLSI BEAMLINE 08B1-1 |
| Synchrotron site | CLSI |
| Beamline | 08B1-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-06-04 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 64.520, 87.260, 66.150 |
| Unit cell angles | 90.00, 94.01, 90.00 |
Refinement procedure
| Resolution | 39.674 - 2.400 |
| R-factor | 0.2083 |
| Rwork | 0.207 |
| R-free | 0.22850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1G6G; 3QBZ |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.733 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.674 | 2.600 |
| High resolution limit [Å] | 2.250 | 2.200 |
| Number of reflections | 36580 | |
| <I/σ(I)> | 8.15 | |
| Completeness [%] | 98.3 | 97.4 |
| Redundancy | 2.8 | 2.8 |
| CC(1/2) | 0.990 | 0.318 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 277 | 100 mM TRIS pH 8.5 12.5 % PEG 3350 (v/v) |
