4OIW

Structural and kinetic bases for the metal preference of the M18 aminopeptidase from Pseudomonas aeruginosa

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL45PX
Synchrotron site	SPring-8
Beamline	BL45PX
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2009-02-24
Detector	RIGAKU RAXIS V
Wavelength(s)	1.7321
Spacegroup name	C 2 2 21
Unit cell lengths	150.020, 218.267, 172.693
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.790 - 2.440
R-factor	0.15044
Rwork	0.148
R-free	0.19650
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4njr
RMSD bond length	0.015
RMSD bond angle	1.743
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.640
High resolution limit [Å]	2.440	2.550
Number of reflections	95594
Completeness [%]	99.1	99.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	microbatch Crystallization	7.5	295	30%(v/v) 2-Propanol, 0.1M Hepes 7.5, 0.2M MgCl2, 10mM Spermidine, 0.1mM ZnCl2, microbatch Crystallization, temperature 295K