4EJ1
Binding of Nb113 camelid antibody fragment with the binary DHFR:folate complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-06-15 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0723 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 100.741, 77.064, 92.777 |
Unit cell angles | 90.00, 92.00, 90.00 |
Refinement procedure
Resolution | 19.863 - 1.750 |
R-factor | 0.1883 |
Rwork | 0.186 |
R-free | 0.22350 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.114 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.7.3_928)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.774 |
High resolution limit [Å] | 1.750 | 1.750 |
Number of reflections | 72438 | |
Completeness [%] | 95.3 | 95.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.4 | 293 | 30% PEG1000, 100 mM phosphate/citrate, 110 mM Lithium Citrate, pH 4.4, VAPOR DIFFUSION, SITTING DROP, temperature 293K |