3UQA

Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with surface mutation A54E 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 QUANTUM 315r
Wavelength(s)	0.9774
Spacegroup name	C 1 2 1
Unit cell lengths	96.310, 31.280, 74.320
Unit cell angles	90.00, 121.57, 90.00

Refinement procedure

Resolution	19.720 - 1.550
R-factor	0.182
Rwork	0.182
R-free	0.19300
Structure solution method	MR
Starting model (for MR)	3uf8
RMSD bond length	0.012
RMSD bond angle	1.553
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	1.590
High resolution limit [Å]	1.550	6.930	1.550
Rmerge	0.044	0.017	0.475
Number of reflections	27730	326	2025
<I/σ(I)>	17.26	44.6	3.1
Completeness [%]	99.4	91.1	99.8
Redundancy	3.97

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	290	Internal tracking number 226422. JCSG well A9. 0.2M Ammonium Chloride, 20.0% w/v PEG3500, 30% PEG400 Cryo. BupsA.00130.a.D220 PD00197 19.3mg/ml., pH 7.00, vapor diffusion, sitting drop, temperature 290K