3WT1
Crystal structure of the b'-a' domain of thermophilic fungal protein disulfide isomerase (reduced form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE BL13B1 |
| Synchrotron site | NSRRC |
| Beamline | BL13B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-08-03 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 1 |
| Unit cell lengths | 65.770, 67.750, 70.250 |
| Unit cell angles | 105.92, 113.13, 96.59 |
Refinement procedure
| Resolution | 20.000 - 1.850 |
| R-factor | 0.24 |
| Rwork | 0.238 |
| R-free | 0.27800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2kp1 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.672 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.880 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.055 | 0.378 |
| Number of reflections | 81751 | |
| <I/σ(I)> | 26.2 | 1.5 |
| Completeness [%] | 92.3 | 81.7 |
| Redundancy | 2.1 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 293 | 36% PEG2000MME, 100mM sodium acetate pH 4.6, 200mM ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
