1AUG

CRYSTAL STRUCTURE OF THE PYROGLUTAMYL PEPTIDASE I FROM BACILLUS AMYLOLIQUEFACIENS

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	300
Detector technology	AREA DETECTOR
Collection date	1996-02
Detector	XUONG-HAMLIN MULTIWIRE
Spacegroup name	P 1 21 1
Unit cell lengths	78.712, 80.800, 69.157
Unit cell angles	90.00, 92.75, 90.00

Refinement procedure

Resolution	30.000 - 2.000
R-factor	0.216 *
Rwork	0.197
R-free	0.26000 *
Structure solution method	SIRAS
RMSD bond length	0.011 *
RMSD bond angle	2.210 *
Data scaling software	SCALEPACK
Phasing software	PHASES
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.020
High resolution limit [Å]	1.930	1.930
Rmerge	0.060 *
Number of reflections	50037
<I/σ(I)>	19.82	4.09
Completeness [%]	84.4 *	15.1
Redundancy	2.3 *	1.13

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5		pH 6.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7 (mg/ml)
2	1	reservoir	sodium cacodylate/KH2PO4	0.05 (M)
3	1	reservoir	magnesium acetate	0.1 (M)
4	1	reservoir	PEG4000	10 (%(w/v))