5AUM
Crystal structure of a Fab fragment with the ligand peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL32XU |
| Synchrotron site | SPring-8 |
| Beamline | BL32XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-01-24 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 217.768, 217.768, 52.236 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 45.690 - 2.050 |
| R-factor | 0.19076 |
| Rwork | 0.189 |
| R-free | 0.22055 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bfo |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.511 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.120 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.491 | |
| Number of reflections | 88376 | |
| <I/σ(I)> | 26.4 | 5.1 |
| Completeness [%] | 99.5 | 98.9 |
| Redundancy | 5.3 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 20 % PEG 2000 MME, 0.5 M NaCl, 0.1 M Tris-HCl pH7.0 |
