2P42
Complex of a camelid single-domain vhh antibody fragment with RNASE A at 1.8A resolution: SE3-mono-2 crystal form with three se-met sites (M34, M51, M83) in vhh scaffold
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-04-01 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.97955, 0.97936 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 69.545, 55.002, 65.705 |
Unit cell angles | 90.00, 100.21, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.800 |
R-factor | 0.17275 |
Rwork | 0.171 |
R-free | 0.21544 |
Structure solution method | MAD |
RMSD bond length | 0.013 |
RMSD bond angle | 1.131 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 |
High resolution limit [Å] | 1.800 |
Rmerge | 0.095 |
Number of reflections | 44260 |
Completeness [%] | 98.1 |
Redundancy | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 295 | HAMPTON RESEARCH INDEX SCREEN, SOLUTION #85: MGCL2, PEG3350, HEPES BUFFER, PH 7.5, VAPOR DIFFUSION, temperature 295K |