1OTP
STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE
Experimental procedure
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1990-01 |
Detector | RIGAKU RAXIS |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 78.000, 97.400, 137.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.800 |
R-factor | 0.201 |
Rwork | 0.201 |
R-free | 0.24800 |
Structure solution method | SINGLE ISOMORPHOUS REPLACEMENT |
RMSD bond length | 0.009 * |
RMSD bond angle | 22.300 * |
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] | 79.500 | 2.670 |
High resolution limit [Å] | 2.600 | 2.580 |
Rmerge | 0.071 * | |
Total number of observations | 57343 * | |
Number of reflections | 14713 | |
Completeness [%] | 87.3 | 65.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.6 * | PROTEIN WAS CRYSTALLIZED FROM 0.9 - 1.2 M SODIUM CITRATE (PH 6.4 - 6.8) AND 2MM DTT AT ROOM TEMPERATURE USING HANGING DROP METHOD |
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) |