6O49

CRYSTAL STRUCTURE OF SMT FUSION PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM BURKHOLDERIA PSEUDOMALLEI COMPLEXED WITH SF339

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	PIXEL
Collection date	2018-01-12
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97949
Spacegroup name	P 1 21 1
Unit cell lengths	58.860, 33.600, 98.140
Unit cell angles	90.00, 101.21, 90.00

Refinement procedure

Resolution	48.130 - 1.850
R-factor	0.171
Rwork	0.168
R-free	0.21100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	BE4 model
RMSD bond length	0.006
RMSD bond angle	0.766
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((1.13_2998: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.130	1.900
High resolution limit [Å]	1.850	1.850
Rmerge	0.089	0.398
Rmeas	0.106	0.054
Number of reflections	31913	405
<I/σ(I)>	9.91	2.63
Completeness [%]	97.4	80.4
Redundancy	3.212	2.98
CC(1/2)	0.994	0.995

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	289	BupsA.00130.a.D21 (CID4597, SMT tag on, Batch 1264062) at 10.37mg/ml (in 25mM Tris, pH8.0, 200mM NaCl, 1% glycerol, 1mM TCEP buffer) was incubated with 2mM SF339_S (BSI5671). Crystals were produced by sitting drop vapor diffusion with an equal volume combination of the protein/ligand complex and a solution containing 100 mM MES pH 6.0, 200 mM Calcium chloride dehydrate, 20% PEG6000 (PACT B11). Crystal Tracking ID 297348b11, izs6-2