1HLW
STRUCTURE OF THE H122A MUTANT OF THE NUCLEOSIDE DIPHOSPHATE KINASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 75.001, 75.001, 106.169 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 1.900 |
R-factor | 0.166 |
Rwork | 0.166 |
R-free | 0.20800 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.900 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (0.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.020 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.069 | |
Total number of observations | 110350 * | |
Number of reflections | 13910 | |
Completeness [%] | 95.8 | 88 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 290 | PEG 600, Magnesium Chloride, Tris Hydrochloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | PEG600 | 10 (%) | |
2 | 1 | drop | 20 (mM) | ||
3 | 1 | drop | Tris-HCl | 50 (mM) | |
4 | 1 | drop | protein | 12.5 (mg/ml) | |
5 | 1 | reservoir | PEG600 | 20 (%) | |
6 | 1 | reservoir | 20 (mM) | ||
7 | 1 | reservoir | Tris-HCl | 50 (mM) |