4N17

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU300
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2013-09-17
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.54
Spacegroup name	C 2 2 21
Unit cell lengths	96.152, 101.369, 55.720
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.415 - 1.501
R-factor	0.1719
Rwork	0.170
R-free	0.20150
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4lnm
RMSD bond length	0.015
RMSD bond angle	1.338
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	HKL-3000
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	100.000	100.000	1.530
High resolution limit [Å]	1.500	4.070	1.500
Rmerge	0.070	0.040	0.588
Number of reflections	43587
<I/σ(I)>	12
Completeness [%]	99.4	98.9	91.8
Redundancy	8	8.5	4.4

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-galacturonic acid, reservoir: 0.2 M calcium acetate, 0.1 M MES, pH 6.0, 20% w/v PEG8000 (MCSG1 B6), cryoprotection: 4:1 50% w/v PEG3350:reservoir, VAPOR DIFFUSION, SITTING DROP, temperature 298K