4G50

Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with surface mutation D44G from Burkholderia pseudomallei complexed with CJ168

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2012-05-26
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9774
Spacegroup name	P 1
Unit cell lengths	33.630, 35.110, 75.150
Unit cell angles	91.54, 99.90, 97.23

Refinement procedure

Resolution	37.000 - 1.750
R-factor	0.172
Rwork	0.170
R-free	0.21900
Structure solution method	MR
Starting model (for MR)	4fn2
RMSD bond length	0.016
RMSD bond angle	1.533
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	37.000	37.000	1.800
High resolution limit [Å]	1.750	7.830	1.750
Rmerge	0.055	0.018	0.520
Number of reflections	32845	379	2356
<I/σ(I)>	16.44	52.5	2.5
Completeness [%]	97.1	99.2	95.5
Redundancy	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	295	Internal tracking number 233897a9. Puck VKT6-9, JCSG_A8 optimization. 50mM Ammonium formate, 24.55% PEG 3,350, 10% ethylene glycol. BupsA.00130.a.D214, 20.00 mg/ml, CJ168 (EBSI2861), pH 7.5, vapor diffusion, sitting drop, temperature 295K