2V3X

His243Ala Escherichia coli aminopeptidase P in complex with substrate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	CCD
Collection date	2006-04-23
Detector	ADSC CCD
Spacegroup name	P 64 2 2
Unit cell lengths	177.396, 177.396, 96.499
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.060 - 1.700
R-factor	0.141
Rwork	0.141
R-free	0.15400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1wl9
RMSD bond length	0.011
RMSD bond angle	1.288
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	REFMAC
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.060	0.340
Number of reflections	95461
<I/σ(I)>	20.9	4.4
Completeness [%]	97.7	98.3
Redundancy	4.6	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	277	CRYSTALLISED IN 30% PEG 4K, 0.1 M TRIS PH 8.5 AT 277K. SOAKED IN 30% PEG 4K, 0.1 M TRIS PH 8.5, 1 MM MNCL2, 5 MM VAL-PRO-LEU, 10% MPD FOR 30 MIN AT 277K IMMEDIATELY PRIOR TO DATA COLLECTION.