1I4Z

THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII L98Y METHEMERYTHRIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1998-08-08
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 1 21 1
Unit cell lengths	54.083, 129.991, 71.413
Unit cell angles	90.00, 111.22, 90.00

Refinement procedure

Resolution	66.570 - 2.100
R-factor	0.23 *
Rwork	0.248
R-free	0.31100
Structure solution method	Difference Fourier Analysis
Starting model (for MR)	Phascolopsis gouldii wild type methemerythrin
RMSD bond length	0.015
RMSD bond angle	1.400
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	66.570	2.230
High resolution limit [Å]	2.100	2.100
Rmerge	0.079	0.280
Number of reflections	45724
<I/σ(I)>	4.18
Completeness [%]	85.3	67.2
Redundancy	1.43	1.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	281	PEG 4000, glycerol, HEPES, sodium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 281K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mgHr/mL)
2	1	reservoir	PEG4000	20 (%(w/v))
3	1	reservoir	glycerol	25 (%(w/v))