5LRJ
Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin C 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 | 2006-09-11 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.934 |
Spacegroup name | P 32 |
Unit cell lengths | 124.960, 124.960, 48.120 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 48.120 - 2.200 |
Rwork | 0.152 |
R-free | 0.21000 |
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] | 48.120 | 2.270 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.076 | 0.321 |
Number of reflections | 42541 | |
<I/σ(I)> | 12.7 | |
Completeness [%] | 99.7 | 99.5 |
Redundancy | 3.1 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 293 | 1 ul of a solution of 16 mg/ml CPB with 40 mM epsilon-amino caproic acid in water was equilibrated against 14-20% PEG8000 in 100 mM MES (pH 6.0) using a hanging drop Setup. |