2TPT
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 | SIEMENS |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 132.000, 132.000, 67.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.600 |
R-factor | 0.207 |
Rwork | 0.207 |
R-free | 0.24400 |
Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 21.800 * |
Data reduction software | XENGEN |
Data scaling software | XENGEN |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 66.000 | 2.670 |
High resolution limit [Å] | 2.600 | 2.580 |
Rmerge | 0.077 * | |
Total number of observations | 93897 * | |
Number of reflections | 18521 | |
Completeness [%] | 95.7 * | 86.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.5 | Cook, W.J.,(1987) J. Biol. Chem., 262, 3788. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 52 (mg/ml) | |
2 | 1 | drop | ammonium sulfate | 35 (%) | |
3 | 1 | drop | citrate | 0.05 (M) | |
4 | 1 | reservoir | ammonium sulfate | 35 (%) | |
5 | 1 | reservoir | citrate | 0.05 (M) |