1FR5

PHAGE FR CAPSIDS WITH A FOUR RESIDUE DELETION IN THE COAT PROTEIN FG LOOP

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1997-01-21
Detector	MARRESEARCH
Spacegroup name	H 3 2
Unit cell lengths	264.100, 264.100, 654.200
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 3.500
R-factor	0.256
Rwork	0.256
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1frs
RMSD bond length	0.016
RMSD bond angle	26.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.560
High resolution limit [Å]	3.500	3.500
Rmerge	0.139	0.387
Number of reflections	52800	1419 *
<I/σ(I)>	6.9
Completeness [%]	48.0	26

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	ammonium sulfate	10 (%sat)
2	1	drop	Mops	50 (mM)
3	1	drop		0.02 (%(w/v))
4	1	reservoir	ammonium sulfate	30 (%sat)
5	1	reservoir	Mops	50 (mM)