5LRG
Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin B complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-03-09 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.934 |
Spacegroup name | P 32 |
Unit cell lengths | 124.780, 124.780, 48.900 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 54.040 - 2.020 |
Rwork | 0.176 |
R-free | 0.22900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nsa |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | CNX |
Refinement software | CNX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 54.040 | 2.080 |
High resolution limit [Å] | 2.020 | 2.020 |
Rmerge | 0.099 | 0.331 |
Number of reflections | 54773 | |
<I/σ(I)> | 10.6 | 3.4 |
Completeness [%] | 98.1 | 97.6 |
Redundancy | 2.9 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 1ul 16 mg/ml Protein with 40 mM Epsilon-amino caproic acid in water was equilibrated agains 14-20% PEG8000, 100 mM K-Cacodylate, pH 6.5 in a hanging drop Setup. The complex was prepared by soaking a CPB Crystal overnight in a drop of Reservoir solution with 10 mM Anabaenopeptin. |