3AZQ
Crystal structure of puromycin hydrolase S511A mutant complexed with PGG
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-12-07 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 84.430, 142.680, 156.310 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.800 - 2.700 |
| R-factor | 0.193 |
| Rwork | 0.193 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3azo |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS (1.2) |
| Refinement software | CNS (1.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.119 | 0.407 |
| Number of reflections | 52360 | |
| <I/σ(I)> | 10.6 | 2.5 |
| Completeness [%] | 99.1 | 98.6 |
| Redundancy | 4.4 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 298 | 1.7M ammonium sulfate, 0.1M Tris-HCl , pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
