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.