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 |