5EMX
Crystal structure of the S. cerevisiae Rtf1 histone modification domain mutant R124A R126A R128A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X25 |
Synchrotron site | NSLS |
Beamline | X25 |
Temperature [K] | 110 |
Detector technology | PIXEL |
Collection date | 2011-07-13 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.1 |
Spacegroup name | H 3 2 |
Unit cell lengths | 94.271, 94.271, 76.842 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 14.626 - 1.399 |
R-factor | 0.1436 |
Rwork | 0.142 |
R-free | 0.17800 |
Structure solution method | SAD |
RMSD bond length | 0.009 |
RMSD bond angle | 1.004 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AutoSol |
Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.340 |
High resolution limit [Å] | 1.320 | 1.320 |
Rmerge | 0.051 | 0.626 |
Number of reflections | 30553 | |
<I/σ(I)> | 77.79 | 1.3 |
Completeness [%] | 98.3 | 78.5 |
Redundancy | 13.7 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1M phosphate-citrate (pH 4.2) and 40% PEG 300 |