4DZ2

Crystal structure of a Peptidyl-prolyl cis-trans isomerase with surface mutation R92G from Burkholderia pseudomallei complexed with FK506

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	CCD
Collection date	2011-10-04
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	106.440, 49.050, 66.640
Unit cell angles	90.00, 123.05, 90.00

Refinement procedure

Resolution	44.610 - 2.000
R-factor	0.22
Rwork	0.219
R-free	0.24700
Structure solution method	MR
Starting model (for MR)	3vaw
RMSD bond length	0.015
RMSD bond angle	1.473
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]	44.610		2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.047	0.034	0.131
Number of reflections	19250	234	1392
<I/σ(I)>	26.88	48.6	9.1
Completeness [%]	97.5	95.1	96.6
Redundancy	6.44

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	Internal tracking number 224744. JCSG well D10. 0.1M Cacodylate pH 6.5, 200mM Calcium Acetate, 30.0% w/v PEG400, 20% Ethylene Glycol Cryo. BupsA.00130.a.D239 PD00214 21.8mg/ml, vapor diffusion, sitting drop, temperature 290K, VAPOR DIFFUSION, SITTING DROP