3VAW

Crystal structure of a smt fusion peptidyl-prolyl cis-trans isomerase with surface mutation v3i 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	2011-11-17
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9774
Spacegroup name	P 1 21 1
Unit cell lengths	30.940, 31.380, 81.260
Unit cell angles	90.00, 95.03, 90.00

Refinement procedure

Resolution	40.470 - 1.550
R-factor	0.166
Rwork	0.164
R-free	0.19400
Structure solution method	MR
Starting model (for MR)	3uqa
RMSD bond length	0.012
RMSD bond angle	1.580
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]	40.470		1.590
High resolution limit [Å]	1.550	6.930	1.550
Rmerge	0.036	0.023	0.151
Number of reflections	22306	268	1170
<I/σ(I)>	24.33	48.4	4.8
Completeness [%]	97.3	91.2	70.5
Redundancy	3.88

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	Internal tracking number 226593. PACT well H3. 0.2M Sodium Iodide, 0.1M Bis-Tris Propane, pH 8.5, 20.0% w/v PEG3350, 30% PEG400 Cryo. BupsA.00130.a.D24 PD00194 19.6mg/ml., vapor diffusion, sitting drop, temperature 290K