2PRQ

X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-D
Synchrotron site	APS
Beamline	14-BM-D
Temperature [K]	100
Detector technology	CCD
Collection date	1999-03-03
Detector	ADSC QUANTUM 1
Spacegroup name	P 61 2 2
Unit cell lengths	106.200, 106.200, 96.700
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.150
R-factor	0.224
Rwork	0.224
R-free	0.27300
Structure solution method	Model derived phases
Starting model (for MR)	PDB code 1AMP
RMSD bond length	0.008
RMSD bond angle	1.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.230
High resolution limit [Å]	2.150	2.150
Rmerge	0.120	0.743
Number of reflections	18085
<I/σ(I)>	6.5
Completeness [%]	99.9	100

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	298	100 mM Tris pH 8.0, 100 mM KSCN, 4.5 M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 298KK