6CT6
Crystal structure of lactate dehydrogenase from Eimeria maxima with NADH and oxamate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 12.3.1 |
| Synchrotron site | ALS |
| Beamline | 12.3.1 |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2016-04-20 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.1271 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 83.400, 83.400, 227.100 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.636 - 1.705 |
| R-factor | 0.2019 |
| Rwork | 0.202 |
| R-free | 0.21830 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1t2d |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.689 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.636 | 1.729 |
| High resolution limit [Å] | 1.705 | 1.705 |
| Rmeas | 0.134 | 3.660 |
| Number of reflections | 100328 | 9532 |
| <I/σ(I)> | 6.43 | 0.34 |
| Completeness [%] | 88.7 | 98.5 |
| Redundancy | 1.84 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 20mg/mL protein, 2mM NADH, 2mM oxamate; well solution: 0.1M HEPES, 2.0M ammonium formate; dextrose cryoprotectant prior to flash-freezing in liquid nitrogen |
