5IM2

Crystal structure of a TRAP solute binding protein from Rhodoferax ferrireducens T118 (Rfer_2570, TARGET EFI-510210) in complex with copurified benzoate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 31-ID
Synchrotron site	APS
Beamline	31-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2014-04-09
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	P 21 21 21
Unit cell lengths	51.014, 71.864, 78.603
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.568 - 1.700
R-factor	0.1594
Rwork	0.157
R-free	0.19920
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5i7i
RMSD bond length	0.009
RMSD bond angle	0.979
Data reduction software	MOSFLM
Data scaling software	Aimless (0.1.27)
Phasing software	MOLREP
Refinement software	PHENIX ((1.10.1_2155))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	28.570	28.570	1.730
High resolution limit [Å]	1.700	9.000	1.700
Rmerge	0.121	0.049	0.717
Rmeas	0.130	0.054	0.777
Rpim	0.049	0.022	0.297
Total number of observations	224541	853	11514
Number of reflections	32423
<I/σ(I)>	7.9	13.2	1.8
Completeness [%]	99.7	64.9	100
Redundancy	6.9	5	6.8
CC(1/2)	0.996	0.998	0.801

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.3	298	Protein (10 mM HEPES pH 7.5, 5 mM DTT, 10 mM 3,4-Dihydroxybenzoate); Reservoir (MCSG1 D12, 0.2 M Ammonium Chloride pH 6.3, 20 %(w/v) PEG 3350); Cryoprotection (20% diethylen glycol, 80% reservoir)