3CIA

Crystal structure of cold-aminopeptidase from Colwellia psychrerythraea

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Wavelength(s)	0.9799
Spacegroup name	P 1
Unit cell lengths	81.370, 87.100, 116.360
Unit cell angles	88.83, 70.68, 88.43

Refinement procedure

Resolution	46.680 - 2.700
R-factor	0.25047
Rwork	0.249
R-free	0.27011
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hs6
RMSD bond length	0.026
RMSD bond angle	2.228
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	REFMAC (5.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.700	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.200
Number of reflections	74827
<I/σ(I)>	8.57
Completeness [%]	93.5	67.1
Redundancy	2.29

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	291	23 % w/v PEG 3350, 0.5 M NaCl, 0.1 M Bis-Tris, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 291K