4IHM
G215S, A251G, T257A, D260G, T262D mutant of carboxypeptidase T from Thermoactinomyces vulgaris
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Wavelength(s) | 0.8 |
| Spacegroup name | P 63 2 2 |
| Unit cell lengths | 158.101, 158.101, 104.584 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.000 - 1.290 |
| R-factor | 0.14079 |
| Rwork | 0.140 |
| R-free | 0.14821 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3qnv |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.270 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.290 |
| Number of reflections | 191107 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | COUNTER-DIFFUSION | COUNTER DIFFUSION |
