1V3W

Structure of Ferripyochelin binding protein from Pyrococcus horikoshii OT3

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B1
Synchrotron site	SPring-8
Beamline	BL26B1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2003-09-28
Detector	RIGAKU RAXIS V
Wavelength(s)	1.0
Spacegroup name	F 41 3 2
Unit cell lengths	156.156, 156.156, 156.156
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.500
Rwork	0.185
R-free	0.20300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qq0
RMSD bond length	0.006
RMSD bond angle	26.300 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.550
High resolution limit [Å]	1.500	1.500
Rmerge	0.071	0.111
Total number of observations	120843 *
Number of reflections	26357	2602 *
<I/σ(I)>	6.5	7.9
Completeness [%]	98.7	99.8
Redundancy	4.6	4.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8 *	295	PEG4000, Hepes, CALCIUM CHLORIDE, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	Tris	0.02 (M)	pH8.0
3	1	drop		0.2 (M)
4	1	reservoir	PEG4000	26 (%)	pH7.5