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) |