4N91

Crystal structure of a trap periplasmic solute binding protein from anaerococcus prevotii dsm 20548 (Apre_1383), target EFI-510023, with bound alpha/beta d-glucuronate

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	2013-10-15
Detector	RAYONIX 225 HE
Wavelength(s)	0.9793
Spacegroup name	P 31 2 1
Unit cell lengths	107.216, 107.216, 66.417
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	28.231 - 1.700
R-factor	0.148
Rwork	0.147
R-free	0.17160
Structure solution method	SAD
RMSD bond length	0.011
RMSD bond angle	1.264
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.20)
Phasing software	PHENIX (AUTOSOLVE)
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	92.852	28.231	1.790
High resolution limit [Å]	1.700	5.380	1.700
Rmerge	0.127	0.060	0.759
Total number of observations		33555	141430
Number of reflections	47522
<I/σ(I)>	17.6	9.4	1
Completeness [%]	98.0	98.2	96.9
Redundancy	22	20.8	20.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	298	Protein (42 mg/ml, 10 mM HEPES pH 7.5, 5 mM DTT, 10 mM D-GLUCURONATE); Reservoir (0.2 M Magnesium Chloride, 0.1 M Citrate pH 5.5, 40% (v/v) PEG400); Cryoprotection (100% Reservoir), sitting drop vapor diffusion, temperature 298K, VAPOR DIFFUSION, SITTING DROP