5YUP
Crystal Structure of the Fab fragment of FVIIa antibody mAb4F5
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U1 |
Synchrotron site | SSRF |
Beamline | BL17U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-12-19 |
Detector | DECTRIS PILATUS3 S 6M |
Wavelength(s) | 0.9791 |
Spacegroup name | I 2 3 |
Unit cell lengths | 141.640, 141.640, 141.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 70.820 - 1.810 |
R-factor | 0.209 |
Rwork | 0.207 |
R-free | 0.24900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2BRR AND 2R4R |
RMSD bond length | 0.009 |
RMSD bond angle | 1.310 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.820 | 1.840 |
High resolution limit [Å] | 1.810 | 1.810 |
Rmerge | 0.082 | 1.800 |
Number of reflections | 43048 | 2259 |
<I/σ(I)> | 25.9 | |
Completeness [%] | 100.0 | |
Redundancy | 15 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | 2.3M ammonium sulfate, 100mM Tris-HCl pH 7.4, 5% PEG 400 |