5VLC
Crystal Structure of Medicago truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-12-17 |
Detector | RAYONIX MX300-HS |
Wavelength(s) | 0.97625 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 102.859, 139.201, 102.692 |
Unit cell angles | 90.00, 119.18, 90.00 |
Refinement procedure
Resolution | 48.730 - 1.970 |
R-factor | 0.17888 |
Rwork | 0.179 |
R-free | 0.22912 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1kae |
RMSD bond length | 0.015 |
RMSD bond angle | 1.693 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | BALBES |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.730 | 2.090 |
High resolution limit [Å] | 1.970 | 1.970 |
Rmerge | 0.078 | 0.905 |
Number of reflections | 175983 | 27746 |
<I/σ(I)> | 13.7 | 1.9 |
Completeness [%] | 99.4 | 97.4 |
Redundancy | 6.14 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 292 | 100 mM MES pH 5.2, 200 mM NACl, 12% PEG 3350 |