1DBX
Crystal structure of cysteinyl-tRNA(Pro) deacylase from H. influenzae (HI1434)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12C |
| Synchrotron site | NSLS |
| Beamline | X12C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-10-27 |
| Detector | BRANDEIS |
| Spacegroup name | P 1 |
| Unit cell lengths | 32.560, 42.210, 54.160 |
| Unit cell angles | 109.07, 100.32, 90.62 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| Rwork | 0.183 |
| R-free | 0.25900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | YBAK structure in C2 space group 1dbu |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.032 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.033 | 0.129 |
| Total number of observations | 96443 * | |
| Number of reflections | 49134 | |
| Completeness [%] | 97.6 | 97.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 6 (mg/ml) | |
| 2 | 1 | drop | potassium phosphate | 50 (mM) | |
| 3 | 1 | drop | EDTA | 0.1 (mM) | |
| 4 | 1 | drop | dithiothreitol | 5 (mM) | |
| 5 | 1 | reservoir | Tris-HCl | 100 (mM) | |
| 6 | 1 | reservoir | mPEG5000 | 25-35 (%) | |
| 7 | 1 | reservoir | propanol | 3 (%) |
