1FRS

CRYSTAL STRUCTURE OF BACTERIOPHAGE FR CAPSIDS AT 3.5 ANGSTROMS RESOLUTION

Experimental procedure

Spacegroup name	C 1 2 1
Unit cell lengths	422.900, 305.900, 274.800
Unit cell angles	90.00, 129.80, 90.00

Refinement procedure

Resolution	20.000 - 3.500
R-factor	0.228
Rwork	0.228
R-free	0.23600
RMSD bond length	0.029
RMSD bond angle	3.500 *
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	9.350 *
High resolution limit [Å]	3.470 *	3.470 *
Rmerge	0.137 *	0.283 *
Number of reflections	130705	8708 *
Completeness [%]	38.0	16 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *	20 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	25-28 (mg/ml)
2	1	drop	ammonium sulfate	10 (%sat)
3	1	drop	MOPS	50 (mM)
4	1	drop		0.02 (%(w/v))
5	1	reservoir	ammonium sulfate	30 (%sat)
6	1	reservoir	MOPS	50 (mM)