4I66
Crystal structure of Hoch_4089 protein from Haliangium ochraceum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-10-22 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.97915 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 58.185, 58.185, 94.779 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 22.250 - 1.300 |
R-factor | 0.15991 |
Rwork | 0.159 |
R-free | 0.19843 |
Structure solution method | SAD |
RMSD bond length | 0.017 |
RMSD bond angle | 1.569 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | MLPHARE |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.320 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.086 | 0.848 |
Number of reflections | 46401 | |
<I/σ(I)> | 30.5 | 2.7 |
Completeness [%] | 99.7 | 100 |
Redundancy | 9 | 8.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 297 | 0.2 M Li2SO4, 0.1 M HEPES/NaOH pH 7.5, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 297K |