3HOA
Crystal structure of the Thermus thermophilus M32 carboxypeptidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL1-5 |
| Synchrotron site | SSRL |
| Beamline | BL1-5 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-09-10 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00002 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 58.610, 84.330, 109.050 |
| Unit cell angles | 90.00, 93.75, 90.00 |
Refinement procedure
| Resolution | 19.980 - 2.100 |
| R-factor | 0.223 |
| Rwork | 0.218 |
| R-free | 0.25100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Bacillus subtilis carboxypeptidase |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.200 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.700 | 2.230 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.095 | 0.209 |
| Number of reflections | 60029 | |
| <I/σ(I)> | 20.4 | 5.1 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 3.417 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4 | 298 | 0.1 M Na-citrate pH 4.0, 8% w/v PEG 6000, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
