1C9E

STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	AREA DETECTOR
Collection date	1998-10-25
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	49.840, 58.560, 98.020
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.300
R-factor	0.183 *
Rwork	0.184
R-free	0.25700 *
RMSD bond length	0.013
RMSD bond angle	1.900
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	CNS (0.5)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *	2.340
High resolution limit [Å]	2.300	2.300
Rmerge	0.098	0.280
Number of reflections	12500
Completeness [%]	94.2 *	96.6
Redundancy	0.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5 *	298	used to microseeding *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	subtilis ferrochelatase	1 (mM)
2	1	drop	N-MeMP	1 (mM)
3	1	reservoir	PEG2000	30 (%(w/v))
4	1	reservoir		0.2 (M)
5	1	reservoir	Tris-HCl	100 (mM)
6	1	reservoir		0.5 (mM)