1F9N

CRYSTAL STRUCTURE OF AHRC, THE ARGININE REPRESSOR/ACTIVATOR PROTEIN FROM BACILLUS SUBTILIS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1995-11-04
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	230.310, 73.860, 138.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.700
R-factor	0.22
Rwork	0.220
R-free	0.27000
RMSD bond length	0.004
RMSD bond angle	1.000
Data reduction software	MOSFLM
Data scaling software	CCP4 ((AGROVATA)
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.870
High resolution limit [Å]	2.700	2.700
Rmerge	0.066	0.140
Number of reflections	28055
<I/σ(I)>	10
Completeness [%]	88.7	85.7
Redundancy	1.6	1.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.9	291	PEG 4000, ammonium sulphate, phosphate buffer, protease inhibitors (PMSF, TPCK) in isopropanol, pH 4.9, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	ammonium sulfate	60 (mM)
3	1	reservoir	phosphate	100 (mM)	pH4.9
4	1	reservoir	PEG4000	3 (%(w/v))