1F36

THE CRYSTAL STRUCTURE OF FIS MUTANT K36E REVEALS THAT THE TRANSACTIVATION REGION OF THE FIS PROTEIN CONTAINS EXTENDED MOBILE BETA-HAIRPIN ARMS

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1996-07-16
Detector	RIGAKU RAXIS II
Spacegroup name	P 65 2 2
Unit cell lengths	51.900, 51.900, 294.930
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 2.650
R-factor	0.222
Rwork	0.222
R-free	0.27700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	ORTHORHOMBIC CRYSTAL FORM OF THE LYS36-GLU FIS STRUCTURE
RMSD bond length	0.011
RMSD bond angle	23.720 *
Data reduction software	MSC
Data scaling software	MSC
Phasing software	AMoRE
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.750
High resolution limit [Å]	2.650	2.650
Rmerge	0.069	0.301
Total number of observations	79532 *
Number of reflections	7139
<I/σ(I)>		1.63
Completeness [%]	93.0	55.6
Redundancy	11.1	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.2		CRYSTALS GROWN BY HANGING DROP VAPOR DIFFUSION FROM A SOLUTION OF 20 MG/ML PROTEIN, 500 MM NACL, 10 MM TRIS-HCL, PH 8.2, 2 M NAFORMATE, AGAINST 4 M NAFORMATE AS THE RESERVOIR, vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	sodium formate	2 (M)
3	1	reservoir	sodium formate	4 (M)