3KRS
Structure of Triosephosphate Isomerase from Cryptosporidium Parvum at 1.55A Resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-25 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.976484 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.560, 71.930, 75.830 |
| Unit cell angles | 90.00, 106.47, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.550 |
| R-factor | 0.159 |
| Rwork | 0.157 |
| R-free | 0.18800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2vfd |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.415 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.590 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.077 | 0.364 |
| Number of reflections | 79305 | |
| <I/σ(I)> | 12.93 | 2.9 |
| Completeness [%] | 99.0 | 91.3 |
| Redundancy | 3.6 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 290 | MD PACT SCREEN G8: 20% PEG 3350, 100MM BISTRISPROPANE PH 7.5, 200MM NA2SO4, CRPAA.01119.A AT 75 MG/ML, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K |
