1AA0

FIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1995-07-01
Detector	RIGAKU RAXIS IIC
Spacegroup name	H 3 2
Unit cell lengths	41.200, 41.200, 358.700
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.200
R-factor	0.216
Rwork	0.216
R-free	0.26700 *
Structure solution method	MIR
RMSD bond length	0.010 *
RMSD bond angle	1.300 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.240
High resolution limit [Å]	2.200	2.200
Rmerge	0.053 *
Total number of observations	57901 *
Number of reflections	6490 *
<I/σ(I)>	15	2
Completeness [%]	92.6	56.6
Redundancy	4.8	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	22 *	PROTEIN WAS CRYSTALLIZED AT 22OC USING 34% PEG400, 0.1M ZN ACETATE IN 0.1M MES BUFFER AT PH6.0 AS WELL SOLUTION BY MIXING EQUAL AMOUNT OF WELL SOLUTION AND PROTEIN SOLUTION AT 29MG/ML IN A HANGING DROP, vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	29 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)	pH7.5
3	1	reservoir	PEG400	34 (%)
4	1	reservoir	zinc acetate	0.1 (M)
5	1	reservoir	MES	0.1 (M)	pH6.0