1E2Y
Tryparedoxin peroxidase from Crithidia fasciculata
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-06-15 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.8800,0.9790,0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 123.800, 97.200, 133.800 |
| Unit cell angles | 90.00, 93.10, 90.00 |
Refinement procedure
| Resolution | 21.000 - 3.200 |
| R-factor | 0.273 |
| Rwork | 0.273 |
| R-free | 0.28600 |
| Structure solution method | MAD |
| RMSD bond length | 0.010 |
| RMSD bond angle | 23.410 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 21.000 | 21.000 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.091 * | 0.480 * |
| Total number of observations | 376643 * | |
| Number of reflections | 52094 | |
| <I/σ(I)> | 14.8 | 2.6 |
| Completeness [%] | 99.8 | 96.7 |
| Redundancy | 4 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | drop consists of 2.5 micro litter of protein mixed with 2 micro litter of reservoir solution and 0.5 micro litter EDTA * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 16 (mg/ml) | |
| 2 | 1 | drop | EDTA | 0.1 (M) | |
| 3 | 1 | reservoir | PEG1000 | 12.5 (%(w/v)) | |
| 4 | 1 | reservoir | Tris-HCl | 100 (mM) | |
| 5 | 1 | reservoir | glycerol | 10 (%(v/v)) | |
| 6 | 1 | reservoir | dithiothreitol | 100 (mM) | |
| 7 | 1 | reservoir | DMSO | 0.25 (%(v/v)) |
