1FG3
CRYSTAL STRUCTURE OF L-HISTIDINOL PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH L-HISTIDINOL
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-05-31 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 132.484, 62.435, 45.530 |
Unit cell angles | 90.00, 104.26, 90.00 |
Refinement procedure
Resolution | 45.000 - 2.200 |
R-factor | 0.198 * |
Rwork | 0.198 |
R-free | 0.21800 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.500 * |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.072 | 0.213 |
Total number of observations | 51924 * | |
Number of reflections | 17053 | |
<I/σ(I)> | 11.4 | |
Completeness [%] | 92.6 | 68.7 |
Redundancy | 3 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 292 | PEG 3350, Tris-Hcl, MgCl2, Glycerol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | drop | 200 (mM) | ||
4 | 1 | drop | EDTA | 1 (mM) | |
5 | 1 | reservoir | PEG3350 | 22.5 (%(w/v)) | |
6 | 1 | reservoir | Tris-HCl | 50 (mM) | |
7 | 1 | reservoir | 200 (mM) | ||
8 | 1 | reservoir | glycerol | 7 (%(w/v)) |