5HH7
crystal structure of Arabidopsis ORC1b BAH-PHD cassette in complex with unmodified H3 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-04-04 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.2827 |
Spacegroup name | P 43 |
Unit cell lengths | 64.408, 64.408, 79.633 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.543 - 1.901 |
R-factor | 0.1948 |
Rwork | 0.194 |
R-free | 0.20470 |
Structure solution method | SAD |
RMSD bond length | 0.003 |
RMSD bond angle | 0.858 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 4.090 | 1.900 |
Rmerge | 0.092 | 0.071 | 0.491 |
Total number of observations | 184019 | ||
Number of reflections | 25599 | ||
<I/σ(I)> | 14 | ||
Completeness [%] | 99.8 | 99.6 | 99.6 |
Redundancy | 7.2 | 6.6 | 7.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 0.2M Na-formate and 20% PEG3350 |