4FN2

Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with surface mutation D44G from Burkholderia pseudomallei complexed with CJ37

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, 35.140, 75.640
Unit cell angles	90.86, 99.52, 96.24

Refinement procedure

Resolution	37.280 - 1.950
R-factor	0.175
Rwork	0.172
R-free	0.22400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3uqb
RMSD bond length	0.015
RMSD bond angle	1.551
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]	74.560		2.000
High resolution limit [Å]	1.950	8.720	1.950
Rmerge	0.094	0.028	0.505
Number of reflections	24210	269	1752
<I/σ(I)>	12.27	39.5	2.7
Completeness [%]	97.9	99.3	97
Redundancy	3.82

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	295	Internal tracking number 233926b1. Puck VKT6-6, Morpheus well B1. 10% PEG 20,000, 20% PEG MME550, 0.03M Halides (NaF, NaBr, NaI), 0.1M MES/Imidazole pH 6.5, Direct Cryo. BupsA.00130.a.D214, 20.00 mg/ml, CJ37 (EBSI2854), vapor diffusion, sitting drop, temperature 295K