1AZY
STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH3R |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Collection date | 1990-01 |
Detector | NICOLET |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 52.000, 78.000, 116.500 |
Unit cell angles | 90.00, 91.50, 90.00 |
Refinement procedure
Resolution | 8.000 - 3.000 |
R-factor | 0.213 * |
Rwork | 0.204 |
R-free | 0.27100 * |
Structure solution method | MIR |
RMSD bond length | 0.009 |
RMSD bond angle | 1.300 * |
Data reduction software | XENGEN |
Data scaling software | XENGEN |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.700 | 2.890 |
High resolution limit [Å] | 2.800 | 2.790 |
Rmerge | 0.101 * | |
Total number of observations | 81699 * | |
Number of reflections | 22922 | |
Completeness [%] | 95.7 | 72.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.6 | pH 4.6 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 33 (mg/ml) | |
2 | 1 | drop | PEG4000 | 7.5 (%) | |
3 | 1 | drop | citrate | 50 (mM) | |
4 | 1 | reservoir | PEG4000 | 15 (%) | |
5 | 1 | reservoir | sodium citrate | 50 (mM) |