4GGQ

Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei complexed with CJ40

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	P 1
Unit cell lengths	34.440, 76.150, 76.350
Unit cell angles	95.07, 90.13, 92.65

Refinement procedure

Resolution	38.020 - 1.950
R-factor	0.189
Rwork	0.187
R-free	0.22000
Structure solution method	MR
RMSD bond length	0.015
RMSD bond angle	1.475
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]	38.020	38.020	2.000
High resolution limit [Å]	1.950	8.720	1.950
Rmerge	0.053	0.015	0.507
Number of reflections	54575	610	3990
<I/σ(I)>	12.61	44.5	1.9
Completeness [%]	97.0	98.2	95.8
Redundancy	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	295	Internal tracking number 235051a1. Puck IBH5-4, Morpheus well A1. 10% PEG 20,000, 20% PEG MME550, 0.03M Divalent Catios (MgCl2, CaCl2), 0.1M MES/Imidazole pH 6.5, Direct Cryo. BupsA.00130.a.D21, 20.00 mg/ml, CJ40 (EBSI2855), vapor diffusion, sitting drop, temperature 295K