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.