1I10
HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX7.2 |
Synchrotron site | SRS |
Beamline | PX7.2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-09-13 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.942, 158.542, 266.226 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.300 |
R-factor | 0.2 * |
Rwork | 0.197 |
R-free | 0.25700 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 9ldt |
RMSD bond length | 0.017 |
RMSD bond angle | 1.815 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.400 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.081 | 0.195 |
Number of reflections | 112344 | |
<I/σ(I)> | 14.18 | 5.36 |
Completeness [%] | 92.3 | 89 |
Redundancy | 3.51 | 3.53 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 18 * | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 28 (mg/ml) | |
2 | 1 | drop | NADH | 2.5 (mM) | |
3 | 1 | drop | sodium oxamate | 1 (mM) | |
4 | 1 | drop | HEPES | 100 (mM) | |
5 | 1 | reservoir | PEG8000 | 12 (%) | |
6 | 1 | reservoir | sodium acetate | 100 (mM) | |
7 | 1 | reservoir | sodium HEPES | 100 (mM) |