3CIA
Crystal structure of cold-aminopeptidase from Colwellia psychrerythraea
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Wavelength(s) | 0.9799 |
Spacegroup name | P 1 |
Unit cell lengths | 81.370, 87.100, 116.360 |
Unit cell angles | 88.83, 70.68, 88.43 |
Refinement procedure
Resolution | 46.680 - 2.700 |
R-factor | 0.25047 |
Rwork | 0.249 |
R-free | 0.27011 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hs6 |
RMSD bond length | 0.026 |
RMSD bond angle | 2.228 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.700 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.200 | |
Number of reflections | 74827 | |
<I/σ(I)> | 8.57 | |
Completeness [%] | 93.5 | 67.1 |
Redundancy | 2.29 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 23 % w/v PEG 3350, 0.5 M NaCl, 0.1 M Bis-Tris, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 291K |