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.