2H1N
3.0 A X-ray structure of putative oligoendopeptidase F: crystals grown by vapor diffusion technique
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-04-01 |
Detector | MARMOSAIC 300 mm CCD |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 119.987, 119.987, 249.747 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 3.000 |
R-factor | 0.186 |
Rwork | 0.185 |
R-free | 0.21100 |
Structure solution method | SAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.047 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.047 | 0.360 |
Number of reflections | 42052 | |
<I/σ(I)> | 17.6 | 2.1 |
Completeness [%] | 98.7 | 98.3 |
Redundancy | 5.6 | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | Hampton research SaltRX condition #96: 0.1M Bis-Tris Propane buffer, 60% Tascimate, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.00 |