1ILW

Crystal Structure of Pyrazinamidase/Nicotinamidase of Pyrococcus horikoshii

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-03-01
Detector	MARRESEARCH
Wavelength(s)	1.08
Spacegroup name	P 1 21 1
Unit cell lengths	32.977, 43.418, 55.781
Unit cell angles	90.00, 101.22, 90.00

Refinement procedure

Resolution	20.000 - 2.050
R-factor	0.181 *
Rwork	0.181
R-free	0.25700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	a structure of the same protein obtained on MAD data
RMSD bond length	0.007 *
RMSD bond angle	1.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.110
High resolution limit [Å]	2.050	2.050
Rmerge	0.027 *	0.093 *
Number of reflections	9862
<I/σ(I)>	42.5	17.4
Completeness [%]	99.2	88
Redundancy	4.246	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	298	22.5% PEG3350, 250 mM ammonium acetate, 100 mM sodium acetate, pH 4.6. Seeding., VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)	pH7.5
3	1	drop	EDTA	1 (mM)
4	1	reservoir	sodium acetate	100 (mM)	pH4.6
5	1	reservoir	ammonium sulfate	250 (mM)
6	1	reservoir	PEG3350	22.5 (%)