4N15

Crystal structure of a TRAP periplasmic solute binding protein from Burkholderia ambifaria (BAM_6123), Target EFI-510059, with bound beta-D-glucuronate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2013-09-21
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.54
Spacegroup name	C 2 2 21
Unit cell lengths	96.190, 101.781, 55.522
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	22.067 - 1.651
R-factor	0.1603
Rwork	0.158
R-free	0.19550
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ln5
RMSD bond length	0.011
RMSD bond angle	1.273
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	100.000	100.000	1.680
High resolution limit [Å]	1.650	4.480	1.650
Rmerge	0.064	0.028	0.365
Number of reflections	32282
<I/σ(I)>	14.5
Completeness [%]	97.6	89.4	90
Redundancy	4.6	4.9	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	298	59.1 mg/mL protein in 10 mM HEPES, pH 7.5, 5 mM DTT, 10 mM D-glucuronic acid, reservoir: 0.2 M magnesium acetate, 20% w/v PEG3350 (MCSG1 C5), cryoprotection: 4:1 50% w/v PEG3350:reservoir, VAPOR DIFFUSION, SITTING DROP, temperature 298K