1LD3

Crystal Structure of B. subilis ferrochelatase with Zn(2+) 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	IMAGE PLATE
Collection date	1998-10-25
Detector	MARRESEARCH
Wavelength(s)	0.98600
Spacegroup name	P 21 21 21
Unit cell lengths	48.636, 49.876, 118.532
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 * - 2.600
R-factor	0.217
Rwork	0.217
R-free	0.27400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1doz
RMSD bond length	0.008
RMSD bond angle	21.300 *
Data reduction software	XDS
Data scaling software	XDS
Phasing software	CNS (1.1)
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000 *	2.800
High resolution limit [Å]	2.600	2.600
Rmerge	0.128 *	0.342 *
Number of reflections	9203 *
Completeness [%]	95.9 *	97.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	298	Hansson, M., (1995) Proteins: Struct.,Funct., Genet., 23, 607. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	0.65 (mg/ml)
2	1	drop	PEG2000	2.5 (%)
3	1	drop		17 (mM)
4	1	drop	Tris-HCl	8 (mM)
5	1	reservoir	PEG2000	30 (%(w/v))
6	1	reservoir		0.2 (M)
7	1	reservoir	Tris-HCl	0.1 (M)