3QYC
Structure of a dimeric anti-HER2 single domain antibody
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL13B1 |
Synchrotron site | NSRRC |
Beamline | BL13B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-11-06 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 39.805, 76.989, 81.358 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.600 |
R-factor | 0.2092 |
Rwork | 0.209 |
R-free | 0.22900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 1.375 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.052 | 0.052 |
Number of reflections | 33598 | |
Completeness [%] | 99.4 | 99.4 |
Redundancy | 6.4 | 6.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 298 | 20% PEG 6000, 0.1M Bicine, pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |