2BX7
Crystal structure of L. lactis dihydroorotate dehydrogense A in complex with 3,5-dihydroxybenzoate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 53.710, 108.127, 66.216 |
| Unit cell angles | 90.00, 104.06, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.040 |
| R-factor | 0.187 |
| Rwork | 0.184 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ovd |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.528 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.080 |
| High resolution limit [Å] | 2.030 | 2.030 |
| Rmerge | 0.080 | 0.340 |
| Number of reflections | 47526 | |
| <I/σ(I)> | 21.5 | 6.3 |
| Completeness [%] | 93.1 | 47.5 |
| Redundancy | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.8 | HANGING DROPS OF 2 MICROLITERS PROTEIN AND INHIBITOR (17 MG/ML PROTEIN AND 2.6 MM 3, 5-DIHYDROXYBENZOATE) AND 2 MIKROLITERS RESERVOIR. DROPS WERE EQUILIBRATED OVER 1 ML RESERVOIR SOLUTION. RESERVOIR SOLUTION: 30 % PEG 6000, 1 MM DTT, 0.2 M SODIUM ACETATE AND 0.1 M TRIS-HCL, PH 8.8 |
