1IPS

ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)

Experimental procedure

Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID2
Synchrotron site	ESRF
Beamline	ID2
Temperature [K]	290
Detector technology	IMAGE PLATE
Collection date	1994-09
Detector	MAR scanner 300 mm plate
Spacegroup name	P 21 21 21
Unit cell lengths	59.200, 127.000, 139.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.500
R-factor	0.22
Rwork	0.220
R-free	0.26500
Structure solution method	MIR
RMSD bond length	0.010
RMSD bond angle	24.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	24.500	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.125	0.379
Total number of observations	136252 *
Number of reflections	36775
<I/σ(I)>	17.6	6.8
Completeness [%]	98.6	96.7
Redundancy	2.3	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5	18 *	used to seeding, Roach, P.L., (1995) Protein Sci., 4, 1007. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	PEG8000	24 (%)
2	1	drop		5 (mM)
3	1	drop	Tris-HCl	100 (mM)
4	1	reservoir	Tris-HCl	100 (mM)
5	1	reservoir	PEG8000	16 (%)