4FYC
Structural and functional characterizations of a thioredoxin-fold protein from Helicobacter pylori
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-1A |
| Synchrotron site | Photon Factory |
| Beamline | BL-1A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-12-10 |
| Detector | ADSC QUANTUM 270 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 140.858, 43.953, 76.699 |
| Unit cell angles | 90.00, 112.29, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.310 |
| R-factor | 0.19303 |
| Rwork | 0.191 |
| R-free | 0.23804 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4fyb |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.202 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 |
| High resolution limit [Å] | 2.300 |
| Number of reflections | 17837 |
| Completeness [%] | 93.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | 200mM sodium formate (pH 7.0), 20% (w/v) PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
