3H3F
Rabbit muscle L-lactate dehydrogenase in complex with NADH and oxamate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-12-15 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.8162 |
| Spacegroup name | P 1 |
| Unit cell lengths | 65.495, 85.279, 138.526 |
| Unit cell angles | 98.49, 91.67, 111.59 |
Refinement procedure
| Resolution | 60.000 - 2.380 |
| R-factor | 0.16207 |
| Rwork | 0.160 |
| R-free | 0.20676 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1i10 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 2.088 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 60.000 | 2.470 |
| High resolution limit [Å] | 2.380 | 2.380 |
| Rmerge | 0.077 | 0.337 |
| Number of reflections | 98703 | |
| <I/σ(I)> | 10.5 | 2 |
| Completeness [%] | 89.9 | 55.6 |
| Redundancy | 2.4 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 16% PEG 8K, Tris buffer, pH7.5, Sodium acetate 0.1M, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
