8VEV
Structure of a mouse IgG antibody antigen-binding fragment (Fab) targeting N6-methyladenosine (m6A), an RNA modification, m6A nucleoside ligand
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID30B |
Synchrotron site | ESRF |
Beamline | ID30B |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-06-16 |
Detector | DECTRIS EIGER2 X 9M |
Wavelength(s) | 0.8731 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 83.640, 128.377, 150.476 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.230 - 3.060 |
R-factor | 0.225 |
Rwork | 0.224 |
R-free | 0.25310 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.003 |
RMSD bond angle | 0.559 |
Data reduction software | autoPROC |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | PHENIX (1.21rc1_5109) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 48.230 | 43.230 | 3.180 |
High resolution limit [Å] | 3.060 | 6.360 | 3.060 |
Rmerge | 0.078 | 0.040 | 0.416 |
Rmeas | 0.085 | 0.044 | 0.451 |
Rpim | 0.033 | 0.017 | 0.172 |
Number of reflections | 31244 | 3662 | 3399 |
<I/σ(I)> | 16.8 | 34.8 | 4 |
Completeness [%] | 99.9 | 99.7 | 100 |
Redundancy | 6.5 | 6.1 | 6.8 |
CC(1/2) | 0.998 | 0.998 | 0.963 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 293 | 0.17 M Ammonium sulfate; 25,5 %(w/v) PEG 4000; 15 %(v/v) Glycerol, 0.2 mM m6A nucleoside |