1AZW

PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	260
Detector technology	IMAGE PLATE
Collection date	1996-09
Detector	MARRESEARCH
Spacegroup name	C 2 2 2
Unit cell lengths	147.200, 167.800, 85.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	7.000 - 2.700
R-factor	0.192
Rwork	0.192
R-free	0.25300
Structure solution method	MULTIPLE ISOMORPHOUS REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.530
Data reduction software	MOSFLM
Data scaling software	CCP4 ((AGROVATA)
Phasing software	SHARP
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall
High resolution limit [Å]	2.700
Rmerge	0.096
Total number of observations	154900 *
Number of reflections	29854
Completeness [%]	93.9
Redundancy	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	6	22 *	drop solution was mixed with an equal volume of reservoir solution *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	Tris-HCl	20 (mM)
3	1	reservoir	sodium azide	0.02 (%(w/v))