3TO1
Two surfaces on Rtt106 mediate histone binding and chaperone activity
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Detector technology | CCD |
Collection date | 2007-08-22 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.11587 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 71.977, 60.703, 76.411 |
Unit cell angles | 90.00, 104.52, 90.00 |
Refinement procedure
Resolution | 23.227 - 2.600 |
R-factor | 0.212 |
Rwork | 0.209 |
R-free | 0.25740 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | model not deposited |
RMSD bond length | 0.012 |
RMSD bond angle | 0.845 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: dev_810)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.227 | 2.740 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 19832 | |
Completeness [%] | 99.8 | 99.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 100mM Hepes pH 7.5, 10% PEG6000, VAPOR DIFFUSION, HANGING DROP, temperature 291K |