3INP

2.05 Angstrom Resolution Crystal Structure of D-ribulose-phosphate 3-epimerase 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	2009-08-05
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	F 41 3 2
Unit cell lengths	224.080, 224.080, 224.080
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.940 - 2.050
R-factor	0.15925
Rwork	0.158
R-free	0.17703
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tqj
RMSD bond length	0.012
RMSD bond angle	1.396
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.090
High resolution limit [Å]	2.050	2.050
Rmerge	0.096	0.472
Number of reflections	30690
<I/σ(I)>	28.2	6.3
Completeness [%]	100.0	100
Redundancy	14.4	14.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4	295	protein solution: 7.5 mg/mL, 0.5M Sodium chloride, TRIS-HCl pH 8.3; Screen solution: JCSG+, condition B1, 0.8M Ammonium sulfate, 0.1M Citric acid pH 4.0; Cryo solution: 1.8M Ammonium sulfate, 25% (w/v) Sucrose., VAPOR DIFFUSION, SITTING DROP, temperature 295K