1PZ5
Structural basis of peptide-carbohydrate mimicry in an antibody combining site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 0.948 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 69.310, 69.310, 198.560 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.970 - 1.800 |
R-factor | 0.219 |
Rwork | 0.219 |
R-free | 0.25400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1m71 |
RMSD bond length | 0.006 * |
RMSD bond angle | 1.500 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.042 | 0.120 |
Total number of observations | 169601 * | |
Number of reflections | 42148 | 2644 * |
<I/σ(I)> | 35.1 | 6.5 |
Completeness [%] | 91.7 | 58.9 |
Redundancy | 4.02 * | 3.65 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.5 | 277 | Vyas, M.N., (1993) J. Mol. Biol., 231, 133. * |