7N04
Crystal structure of the apo F240 antibody fragment
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-12-04 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.9795 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.996, 74.382, 145.041 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.708 - 1.700 |
R-factor | 0.180877855087 |
Rwork | 0.179 |
R-free | 0.22188 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1dfb |
RMSD bond length | 0.010 |
RMSD bond angle | 1.064 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.10_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.710 | 1.760 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.023 | 0.056 |
Number of reflections | 54928 | 4303 |
<I/σ(I)> | 11.6 | |
Completeness [%] | 96.6 | 76.7 |
Redundancy | 2 | |
CC(1/2) | 1.000 | 0.530 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.1 M HEPES-NaOH, pH 7.5, and 20% (w/v) PEG 8000 |