4ND2
Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (pyruvic acid) and cofactor analog (3-acetylpyridine adenine dinucleotide)
Replaces: 2EWDExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-07-03 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9998 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 95.830, 95.830, 185.640 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.610 - 2.000 |
| R-factor | 0.19299 |
| Rwork | 0.191 |
| R-free | 0.20788 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1t2d |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.925 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.054 | 0.186 |
| Number of reflections | 67287 | |
| Completeness [%] | 99.8 | 97.7 |
| Redundancy | 10.7 | 8.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | The protein was incubated with 1 mM pyruvate and 100 uM APAD+ for 1 hour on ice prior to crystallization. Reservoir solution was 1.45-1.65 M ammonium sulfate in 0.1 M sodium cacodylate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
