1DKU

CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7A
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7A
Temperature [K]	285
Detector technology	IMAGE PLATE
Collection date	1996-11-27
Detector	MARRESEARCH
Spacegroup name	P 63
Unit cell lengths	115.650, 115.650, 106.410
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.200
R-factor	0.198
Rwork	0.198
R-free	0.24100
RMSD bond length	0.016
RMSD bond angle	2.011 *
Data scaling software	CCP4 ((AGROVATA)
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.000	1.790
High resolution limit [Å]	2.200 *	2.200 *
Rmerge	0.067 *	0.265 *
Number of reflections	40252 *	7158 *
<I/σ(I)>	4.3
Completeness [%]	98.6 *	98.8 *
Redundancy	3.1	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	293	Sodium citrate, Hepes, alpha,beta-methylene ADP, Magnesium chloride, beta- octylglucoside , pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7 (mg/ml)
2	1	drop	mADP	25 (mM)
3	1	drop		50 (mM)
4	1	drop	beta-octylglucoside	0.5 (%(w/v))
5	1	reservoir	sodium citrate	1 (M)
6	1	reservoir	HEPES	0.1 (M)