7JS3

Structure of the Class II Fructose-1,6-Bisphophatase from Francisella tularensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2017-07-14
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.92456
Spacegroup name	P 1 21 1
Unit cell lengths	76.296, 100.169, 92.021
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	38.110 - 2.400
R-factor	0.155
Rwork	0.153
R-free	0.19300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6ayu
RMSD bond length	0.012
RMSD bond angle	1.500
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0258)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.440
High resolution limit [Å]	2.400	2.400
Rmerge		0.531
Rmeas	0.106	0.531
Rpim		0.276
Number of reflections	53682	2620
<I/σ(I)>	24.6	3.2
Completeness [%]	98.9	97.5
Redundancy	3.6	3.7
CC(1/2)	0.991	0.673

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.8	298	20 mM Tricine pH 7.8, 50 mM KCl, 1 mM MgCl2, 0.1 mM DTT, 15% glycerol; Composition of reservoir solution 0.2 M sodium formate, 20% PEG 3350; Volume and ratio of drop 22.4 uL (1:1) Volume of reservoir (ul) 100