2O1C

Structure of the E. coli dihydroneopterin triphosphate pyrophosphohydrolase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-04-10
Detector	FUJI
Wavelength(s)	1.1
Spacegroup name	C 1 2 1
Unit cell lengths	124.104, 42.579, 106.467
Unit cell angles	90.00, 115.69, 90.00

Refinement procedure

Resolution	95.780 - 1.800
R-factor	0.229
Rwork	0.226
R-free	0.28900
Structure solution method	MIR
RMSD bond length	0.009
RMSD bond angle	1.237
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	SHARP
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	95.945	1.880
High resolution limit [Å]	1.800	1.800
Number of reflections	44935
<I/σ(I)>	10.2
Completeness [%]	95.6	95.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.8	298	1.3-1.5 Ammonium sulfate, 1% propanol, 3-5 mM DTT, 4mM sodium pyrophosphate, 100mM Na Hepes pH 6.8, VAPOR DIFFUSION, SITTING DROP, temperature 298K
1	VAPOR DIFFUSION, SITTING DROP	6.8	298	1.3-1.5 Ammonium sulfate, 1% propanol, 3-5 mM DTT, 4mM sodium pyrophosphate, 100mM Na Hepes pH 6.8, VAPOR DIFFUSION, SITTING DROP, temperature 298K
1	VAPOR DIFFUSION, SITTING DROP	6.8	298	1.3-1.5 Ammonium sulfate, 1% propanol, 3-5 mM DTT, 4mM sodium pyrophosphate, 100mM Na Hepes pH 6.8, VAPOR DIFFUSION, SITTING DROP, temperature 298K