3BJ5
Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X12 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X12 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-11-14 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.89997 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 57.370, 57.370, 68.310 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 18.110 - 2.200 |
| R-factor | 0.19683 |
| Rwork | 0.194 |
| R-free | 0.25525 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.362 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.3.0028) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.690 | 2.260 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.055 | 0.170 |
| Number of reflections | 6879 | |
| <I/σ(I)> | 17.84 | 17.8 |
| Completeness [%] | 99.3 | 99.3 |
| Redundancy | 4.3 | 4.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 295.15 | 2.95M Ammonium sulfate, 0.2M NaCl, 0.1M Tris-HCl pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K |
