4ND1
Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with cofactor (b-nicotinamide adenine dinucleotide) and inhibitor (oxamic acid)
Replaces: 2FNZExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-08-05 |
| Detector | MACSCIENCE |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 94.816, 94.816, 185.072 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.400 - 2.150 |
| R-factor | 0.21119 |
| Rwork | 0.208 |
| R-free | 0.23571 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2EWD |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.954 |
| Data scaling software | d*TREK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.400 | 2.230 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.061 | 0.350 |
| Number of reflections | 50521 | |
| Redundancy | 6.7 | 4.3 |
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 |
