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 |