2PHC
Crystal structure of conserved uncharacterized protein PH0987 from Pyrococcus horikoshii
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-01-31 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97243 |
Spacegroup name | P 61 |
Unit cell lengths | 105.848, 105.848, 51.869 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 18.330 - 2.290 |
R-factor | 0.242 |
Rwork | 0.239 |
R-free | 0.29400 |
Structure solution method | SAD |
RMSD bond length | 0.030 |
RMSD bond angle | 2.581 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE (2.10) |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.380 |
High resolution limit [Å] | 2.290 | 2.290 |
Rmerge | 0.057 | 0.322 |
Number of reflections | 15078 | |
<I/σ(I)> | 28.1 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 15 | 13.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8 | 289 | USING 1.0 MICROLITER DROPS CONTAINING EQUAL VOLUMES OF PROTEIN CONCENTRATE (10.23 mg/mL) IN 20mM Tris-HCl pH 8.0, 1mM DTT, AND SOLUTION CONTAINING 17.5% w/v PEG 3350, 0.2 M Na Iodide, VAPOR DIFFUSION, temperature 289K |