3UF8

Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with a G95A surface mutation from Burkholderia pseudomallei complexed with FK506

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	2011-10-16
Detector	ADSC Q315R
Wavelength(s)	0.9774
Spacegroup name	P 1 21 1
Unit cell lengths	36.400, 32.770, 76.990
Unit cell angles	90.00, 90.59, 90.00

Refinement procedure

Resolution	17.750 - 1.500
R-factor	0.158
Rwork	0.156
R-free	0.18300
Structure solution method	MR, MR
RMSD bond length	0.011
RMSD bond angle	1.530
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	50.000	1.540
High resolution limit [Å]	1.500	6.710	1.500
Rmerge	0.039	0.017	0.301
Number of reflections	29417	347	2145
<I/σ(I)>	23.06	58.4	4.7
Completeness [%]	99.8	93	99.9
Redundancy	4.03

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	290	Internal tracking number 226425. JCSG well A8. 0.2M Ammonium Formate, 20.0% w/v PEG3500, PEG400 Cryo. BupsA.00130.a.D242 PD00198 21.4mg/ml, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 290K