1LBV

Crystal Structure of apo-form (P21) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X8C
Synchrotron site	NSLS
Beamline	X8C
Temperature [K]	100
Detector technology	CCD
Collection date	2000-07-13
Detector	ADSC QUANTUM 4
Wavelength(s)	1.009
Spacegroup name	P 1 21 1
Unit cell lengths	51.812, 53.247, 82.154
Unit cell angles	90.00, 105.05, 90.00

Refinement procedure

Resolution	31.810 - 1.800
R-factor	0.203 *
Rwork	0.203
R-free	0.27300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dk4
RMSD bond length	0.007 *
RMSD bond angle	0.020
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	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.036	0.270 *
Number of reflections	35243 *
<I/σ(I)>	16.8	3.2
Completeness [%]	93.7 *	83.9 *
Redundancy	3.6 *	2.3 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	298	PEG 3350, ammonium phosphate, 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	dihydrogen ammonium phosphate	0.2 (M)
2	1	reservoir	PEG3350	30 (%)
3	1	drop	protein	10 (mg/ml)