2BHA

E. coli Aminopeptidase P in complex with substrate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200H
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2004-10-26
Detector	MARRESEARCH
Spacegroup name	I 41 2 2
Unit cell lengths	138.223, 138.223, 230.841
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	60.190 - 2.400
R-factor	0.178
Rwork	0.177
R-free	0.20400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1N51 STRIPPED OF MULTIPLE CONFORMERS SOLVENT ATOMS AND HETERO COMPOUNDS
RMSD bond length	0.011
RMSD bond angle	1.172
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	0.080	0.630
Number of reflections	43763
<I/σ(I)>	20.2	2.4
Completeness [%]	99.5	99.9
Redundancy	5.1	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	277	AMINOPEPTIDASE P WAS DIALYSED AGAINST EGTA PRIOR TO CRYSTALLISATION. CRYSTALS WERE GROWN USING HANGING DROP VAOPR DIFFUSION AT 4C. RESERVOIR CONTAINED 26% MPD, 100 MM NA.CITRATE (PH 7.5) AND 200 MM MG.ACETATE. CRYSTALS WERE SOAKED IN RESERVOIR SOLUTION SUPPLEMENTED WITH 10 MM VALPROLEU TRIPEPTIDE FOR 1 HOUR AT 4C PRIOR TO DATA COLLECTION.