3UQB

Crystal structure of a SMT Fusion PEPTIDYL-PROLYL CIS-TRANS ISOMERASE with surface mutation D44G 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	P 1 21 1
Unit cell lengths	36.370, 32.640, 77.000
Unit cell angles	90.00, 90.81, 90.00

Refinement procedure

Resolution	19.250 - 1.900
R-factor	0.172
Rwork	0.169
R-free	0.22800
Structure solution method	MR
Starting model (for MR)	3uf8
RMSD bond length	0.012
RMSD bond angle	1.495
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]	38.500		1.950
High resolution limit [Å]	1.900	8.500	1.900
Rmerge	0.070	0.017	0.408
Number of reflections	14527	170	1053
<I/σ(I)>	16.55	54.5	3.4
Completeness [%]	99.8	89.9	99.9
Redundancy	4.02

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	9	290	Internal tracking number 226421. PACT well B6. 0.1M MIB Buffer pH 9.0, 25.0% w/v PEG1500, 30% PEG400 Cryo. BUPSA.00130.A.D214 PD00190/6 23.7mg/ml, vapor diffusion, sitting drop, temperature 290K, VAPOR DIFFUSION, SITTING DROP