4B6Z
Crystal structure of metallo-carboxypeptidase from Burkholderia cenocepacia
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 287 |
Detector technology | CCD |
Collection date | 2011-02-17 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.897, 85.947, 289.016 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.900 |
R-factor | 0.16641 |
Rwork | 0.164 |
R-free | 0.20455 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3k2k |
RMSD bond length | 0.008 |
RMSD bond angle | 1.143 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.130 | 0.480 |
Number of reflections | 124234 | |
<I/σ(I)> | 8.4 | 2.7 |
Completeness [%] | 99.9 | 100 |
Redundancy | 4.2 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 100 NL OF PROTEIN SOLUTION (10 MG ML-1 IN 100 MM SODIUM ACETATE PH 5.0, 150 MM NACL AND 0.5 MM ZINC SULPHATE) WERE MIXED AT 1:1 RATIO WITH RESERVOIR (0.2M LITHIUM SULPHATE, 25% PEG 3350 AND 0.1M BIS-TRIS, PH 5.5) EQUILIBRATED AGAINST A 70 UL RESERVOIR. CRYSTALS WERE OBSERVED AFTER THREE DAYS. |