3CIF
Crystal Structure of C153S mutant glyceraldehyde 3-phosphate dehydrogenase from Cryptosporidium parvum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 103 |
| Detector technology | CCD |
| Collection date | 2005-06-28 |
| Detector | MAR225 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.000, 120.100, 79.280 |
| Unit cell angles | 90.00, 92.08, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.000 |
| R-factor | 0.17921 |
| Rwork | 0.178 |
| R-free | 0.20973 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3CHZ |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.979 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Number of reflections | 84846 | |
| <I/σ(I)> | 11.9 | |
| Completeness [%] | 99.7 | 99.3 |
| Redundancy | 7.1 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 298 | 20% PEG 3000 Prior to crystallization, the protein was incubated with 2 mM NAD and 11 mM D-L-glyceraldehyde 3-phosphate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.50 |
