3ALA
Crystal structure of vascular adhesion protein-1 in space group C2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-06-10 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97946 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 394.468, 115.826, 179.286 |
| Unit cell angles | 90.00, 112.34, 90.00 |
Refinement procedure
| Resolution | 110.400 - 2.900 |
| R-factor | 0.25183 |
| Rwork | 0.250 |
| R-free | 0.28621 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2c10 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.531 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.25) |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 110.430 | 3.060 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.192 | 0.883 |
| Number of reflections | 163097 | |
| <I/σ(I)> | 9.4 | 1.9 |
| Completeness [%] | 98.6 | 98.1 |
| Redundancy | 3.7 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | VAPOR DIFFUSION, SITTING DROP, temperature 293K |
