1K75
The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X8C |
Synchrotron site | NSLS |
Beamline | X8C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-07-15 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.97950,0.97934,0.97857 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.370, 107.520, 157.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.750 |
R-factor | 0.19 * |
Rwork | 0.190 |
R-free | 0.22500 |
Structure solution method | MAD |
RMSD bond length | 0.013 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.780 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.060 * | 0.276 * |
Total number of observations | 402344 * | |
Number of reflections | 91330 * | |
<I/σ(I)> | 11.4 | 2.2 |
Completeness [%] | 97.3 | 79.7 |
Redundancy | 4.4 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 18 * | PEG 3350, glycerol, imidazole/malic acid buffer, ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15.4 (mg/ml) | |
2 | 1 | drop | Tris-Cl | 20 (mM) | pH7.5 |
3 | 1 | drop | 0.2 (M) | ||
4 | 1 | drop | dithiothreitol | 5 (mM) | |
5 | 1 | drop | L-histidine | 1 (mM) | |
6 | 1 | reservoir | PEG3350 | 20 (%(w/v)) | |
7 | 1 | reservoir | glycerol | 7 (%(v/v)) | |
8 | 1 | reservoir | imidazole-malic acid | 0.1 (M) | pH5.5 |
9 | 1 | reservoir | ammonium sulfate | 0.2 (M) |