1XJO

STRUCTURE OF AMINOPEPTIDASE

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12B
Synchrotron site	NSLS
Beamline	X12B
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995-03-25
Detector	MAR scanner 300 mm plate
Spacegroup name	P 41 21 2
Unit cell lengths	61.810, 61.810, 146.300
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.750
R-factor	0.141 *
Rwork	0.141
RMSD bond length	0.020
RMSD bond angle	15.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	TNT (5E)

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000 *
High resolution limit [Å]	1.750 *
Rmerge	0.054
Total number of observations	244396 *
Number of reflections	28606
Completeness [%]	97.0
Redundancy	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8 *		16% PEG 4K, 0.1 M SODIUM ACETATE, pH 5.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	sodium acetate	0.1 (M)
3	1	reservoir	PEG4000	16 (%(w/v))
4	1	drop	Tris	10 (mM)
5	1	drop		20 (mM)
6	1	drop		1 (mM)