4GIV

Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with surface mutation D44G from Burkholderia pseudomallei complexed with CJ183

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	100
Detector technology	CCD
Collection date	2012-06-29
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.976484
Spacegroup name	C 1 2 1
Unit cell lengths	84.420, 32.500, 151.380
Unit cell angles	90.00, 97.52, 90.00

Refinement procedure

Resolution	41.850 - 2.450
R-factor	0.218
Rwork	0.216
R-free	0.26200
Structure solution method	MR
RMSD bond length	0.014
RMSD bond angle	1.612
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.6.0117)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.460
High resolution limit [Å]	2.400	10.730	2.400
Rmerge	0.094	0.038	0.541
Number of reflections	16480	203	1209
<I/σ(I)>	15.96	38.2	4
Completeness [%]	99.9	98.1	100
Redundancy	3.72

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	295	Internal tracking number 232625a12. Puck IBH5-9, JCSG_A8 optimization screen. 50mM Ammonium Formate, 30% PEG3,350, 25% ethylene glycol cryo-protected. BupsA.00130.a.D214, 20.00 mg/ml, CJ183 (EBSI2864), pH 7.5, vapor diffusion, sitting drop, temperature 295K