1EZR
CRYSTAL STRUCTURE OF NUCLEOSIDE HYDROLASE FROM LEISHMANIA MAJOR
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 296 |
Detector technology | AREA DETECTOR |
Collection date | 1997-08-01 |
Detector | SIEMENS |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 81.800, 79.200, 109.800 |
Unit cell angles | 90.00, 91.60, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.500 |
R-factor | 0.205 |
Rwork | 0.203 |
R-free | 0.25500 |
RMSD bond length | 0.007 * |
RMSD bond angle | 0.007 |
Data reduction software | X-GEN |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 * | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.072 | 0.306 |
Total number of observations | 113835 * | |
Number of reflections | 41035 | |
<I/σ(I)> | 10.5 | |
Completeness [%] | 84.1 | 67.7 |
Redundancy | 2.45 | 1.84 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 18 * | PEG 4000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 13-15 (mg/ml) | |
2 | 1 | reservoir | MES | 100 (mM) | |
3 | 1 | reservoir | PEG4000 | 16 (%) |