1LBW

Crystal Structure of apo-form (P32) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-11-02
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 32
Unit cell lengths	89.368, 89.368, 103.558
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.000
R-factor	0.177 *
Rwork	0.186
R-free	0.21200 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dk4
RMSD bond length	0.008 *
RMSD bond angle	0.026
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.040	0.410
Number of reflections	55200 *
<I/σ(I)>	28.1	2.7
Completeness [%]	92.4 *	90.5 *
Redundancy	3.0 *	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	298	PEG 3350, ammonium nitrate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium nitrate	0.2 (M)
2	1	reservoir	PEG3350	30 (%)
3	1	drop	protein	10 (mg/ml)