5C9F
Crystal structure of a retropepsin-like aspartic protease from Rickettsia conorii
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 | 2013-12-14 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 50.102, 94.153, 118.636 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.000 |
R-factor | 0.20034 |
Rwork | 0.199 |
R-free | 0.25452 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.725 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.030 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.510 | |
Number of reflections | 36685 | |
<I/σ(I)> | 30.56 | 1.74 |
Completeness [%] | 94.9 | 64 |
Redundancy | 7.4 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.8 | 293 | 24% PEG4000, 0.2 M lithium sulfate, pH 5.8 |