5LRK

Crystal structure of the porcine carboxypeptidase B - Anabaenopeptin F 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	124.620, 124.620, 48.470
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	62.240 - 2.300
Rwork	0.154
R-free	0.22000
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]	62.240	2.390
High resolution limit [Å]	2.300	2.300
Rmerge	0.080	0.279
Number of reflections	37153
<I/σ(I)>	12.8
Completeness [%]	99.3	99.3
Redundancy	2.9	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	1ul of 16 mg/ml Protein and 40 mM epsilon-amino caproic acid in water were equilibrated against 14-20% PEG8000 and 100 mM K-Cacodylate (pH 6.5) in a hanging drop Setup.