1YTS
A LIGAND-INDUCED CONFORMATIONAL CHANGE IN THE YERSINIA PROTEIN TYROSINE PHOSPHATASE
Experimental procedure
| Collection date | 1992-07-30 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 56.400, 49.800, 100.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.500 |
| R-factor | 0.174 |
| Rwork | 0.174 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 3.700 |
| Data reduction software | SDMS |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.500 * |
| Rmerge | 0.082 * |
| Number of reflections | 9156 |
| Completeness [%] | 92.0 |
| Redundancy | 2.49 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 5.7 * | 296 | MOLECULE: YERSINIA PROTEIN TYROSINE PHOSPHATASE CYS(403)SER COMPLEXED WITH SULFATE. THE CATALYTIC DOMAIN (RESIDUES 163 - 468) OF YOP51 WAS CRYSTALLIZED AT 23 DEGREES CELSIUS, IN A SOLUTION OF 18 - 24% POLYETHYLENE GLYCOL (MW 4000), 5% 2-METHYL-2,4-PENTANEDIOL, 0.1% BETA-MERCAPTOETHANOL, 200MM LI2SO4, 0.1M TRIS-HCL, pH 8.5, temperature 296K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10-12 (mg/ml) | |
| 2 | 1 | drop | 30 (mM) | ||
| 3 | 1 | drop | Na acetate | 5 (mM) | |
| 4 | 1 | drop | PEG4000 | 18-22 (%(w/v)) | precipitant |
| 5 | 1 | drop | 200 (mM) | precipitant | |
| 6 | 1 | drop | 2-propanol | 5 (%) | precipitant |
| 7 | 1 | drop | 2-mercaptoethanol | 0.1 (%) | precipitant |
| 8 | 1 | drop | Tris-HCl | 100 (mM) | precipitant |
| 9 | 1 | reservoir | precipitant | 1 ml |
