2BHB

Zn substituted E. coli Aminopeptidase P

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200H
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2004-12-11
Detector	MARRESEARCH
Spacegroup name	I 41 2 2
Unit cell lengths	138.814, 138.814, 230.914
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	60.190 - 2.410
R-factor	0.168
Rwork	0.167
R-free	0.19000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1N51 STRIPPED OF MULTIPLE CONFORMERS SOLVENT ATOMS AND HETERO COMPOUNDS
RMSD bond length	0.009
RMSD bond angle	1.113
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	60.000	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.070	0.490
Number of reflections	43879
<I/σ(I)>	22.2	3.4
Completeness [%]	98.9	91
Redundancy	6.2	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	277	AMINOPEPTIDASE P WAS DIALYSED AGAINST EGTA PRIOR TO CRYSTALLISATION. CRYSTALS WERE GROWN IN 26% MPD, 100 MM NACITRATE (PH 7.0) AND 200 MM MGACETATE AT 4C BY HANGING DROP VAPOUR DIFFUSION. CRYSTALS WERE SOAKED FOR 2 HOURS IN RESERVOIR SOLUTION SUPPLEMENTED WITH 1 MM ZNCL2 PRIOR TO DATA COLLECTION.