5V8T

Crystal structure of SMT fusion Peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei complexed with SF354

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	CCD
Collection date	2017-01-27
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97949
Spacegroup name	P 1 21 1
Unit cell lengths	60.640, 32.500, 99.350
Unit cell angles	90.00, 96.73, 90.00

Refinement procedure

Resolution	48.915 - 2.100
R-factor	0.1872
Rwork	0.184
R-free	0.22060
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3uf8
RMSD bond length	0.002
RMSD bond angle	0.603
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.915	48.915	2.150
High resolution limit [Å]	2.100	9.390	2.100
Rmerge	0.111	0.026	0.508
Rmeas	0.128	0.030	0.594
Total number of observations	94438
Number of reflections	23040	301	1705
<I/σ(I)>	11.51	34.82	3.18
Completeness [%]	99.8	98.4	99.1
Redundancy	4.099	3.578	3.768
CC(1/2)	0.995	0.999	0.753

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	289	BupsA.00130.a.D21 (CID4597, SMT tag on, Batch 776103) at 10.37mg/ml (in 25mM Tris, pH8.0, 200mM NaCl, 1% glycerol, 1mM TCEP buffer) was incubated with 2mM SF354 (BSI5672). Crystals were produced by sitting drop vapor diffusion with an equal volume combination of the protein/ligand complex and a solution containing 24.55% (w/v) PEG-3350, 50 mM ammonium formate (JCSG_A8 opt screen d7) and cryoprotected with 15% ethylene glycol. Crystal Tracking ID 274545d7, uxe3-7