2V6M
Crystal structure of lactate dehydrogenase from Thermus Thermophilus HB8 (Apo form)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 54.092, 135.296, 85.645 |
Unit cell angles | 90.00, 94.04, 90.00 |
Refinement procedure
Resolution | 29.220 - 2.200 |
R-factor | 0.196 |
Rwork | 0.196 |
R-free | 0.21800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ldn |
RMSD bond length | 0.008 |
RMSD bond angle | 1.100 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.250 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.080 | 0.400 |
Number of reflections | 61724 | |
<I/σ(I)> | 12.29 | 3.38 |
Completeness [%] | 99.6 | 99.8 |
Redundancy | 3.78 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | 0.1M MES PH 6 15% PEG 6000 |