4LN5

Crystal structure of a trap periplasmic solute binding protein from burkholderia ambifaria (Bamb_6123), TARGET EFI-510059, with bound glycerol and chloride ion

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	2013-07-02
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	C 2 2 21
Unit cell lengths	96.098, 97.340, 58.115
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.670 - 2.100
R-factor	0.1574
Rwork	0.154
R-free	0.21990
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2pfy
RMSD bond length	0.007
RMSD bond angle	1.031
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.20)
Phasing software	BALBES
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	68.386	58.115	2.210
High resolution limit [Å]	2.100	6.640	2.100
Rmerge	0.136	0.049	0.668
Total number of observations		3632	16018
Number of reflections	16289
<I/σ(I)>	11.3	12.1	1.2
Completeness [%]	100.0	98.9	100
Redundancy	7.2	6.4	6.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		8.5	298	Protein (16.23 mg/ml, 10 mM HEPES pH 7.5, 150mM NaCl, 5% glycerol, 5 mM DTT), Reservoir (0.8 M Lithium Chloride, 0.1 M Tris pH 8.5, 32%(w/v) PEG 4000 (MCSG1 C9)), Cryoprotection (20% Reservoir, 80% of 50% PEG3350), sitting drop vapor diffusion, temperature 298K