5JQ6
Crystal structure of ClfA in complex with the Fab fragment of Tefibazumab
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] | 120 |
Detector technology | CCD |
Collection date | 2007-03-11 |
Detector | MARRESEARCH |
Wavelength(s) | 0.979 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 234.287, 84.086, 48.626 |
Unit cell angles | 90.00, 98.90, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.400 |
R-factor | 0.21042 |
Rwork | 0.208 |
R-free | 0.25900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2vr3 1f8t |
RMSD bond length | 0.010 |
RMSD bond angle | 1.257 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 2.400 |
Rmerge | 0.090 |
Number of reflections | 36373 |
<I/σ(I)> | 7.3 |
Completeness [%] | 100.0 |
Redundancy | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | PEG 4000, isopropanol, 0.1 M Hepes |