2PNJ

Crystal structure of human ferrochelatase mutant with Phe 337 replaced by Ala

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-BM
Synchrotron site	APS
Beamline	22-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2005-11-18
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.00
Spacegroup name	P 21 21 21
Unit cell lengths	86.686, 94.052, 113.276
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.440 - 2.350
R-factor	0.19473
Rwork	0.192
R-free	0.25332
Structure solution method	DIFFERENCE FOURIER
Starting model (for MR)	1hrk
RMSD bond length	0.016
RMSD bond angle	1.820
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Refinement software	REFMAC (5.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.057	0.242
Number of reflections	58933
<I/σ(I)>	25.23	3.39
Completeness [%]	90.1	98.2
Redundancy	17.5	10

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH	6.5	291	MICROBATCH UNDER OIL (70:30 PARAFFIN/SILICONE OIL MIXTURE) METHO USING 2 microliter DROPS CONTAINING EQUAL VOLUMES OF PROTEIN SOLUTION (64 MG/ML IN 50 MM TRIS MOPS, 0.1M KCL, 1% NA-CHOLATE, 250 MM IMIDAZOLE, PH 8.1) AND PRECIPITANT SOLUTION (0.2 M SODIUM ACETAT TRI HYDRATE, 0.1 M SODIUM CACODYLATE, PH 6.5 IN 30%W/V POLYETHYL GLYCOL 8000 (HAMPTON CRYSTAL SCREEN I-28, HAMPTON RESEARCH), pH 6.50, temperature 291K