4DZ3

Crystal structure of a Peptidyl-prolyl cis-trans isomerase with surface mutation M61H from Burkholderia pseudomallei complexed with FK506

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2012-02-03
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.978720
Spacegroup name	C 2 2 21
Unit cell lengths	48.980, 106.580, 107.160
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.720 - 2.000
R-factor	0.193
Rwork	0.192
R-free	0.21900
Structure solution method	MR
Starting model (for MR)	3vaw
RMSD bond length	0.015
RMSD bond angle	1.518
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]	47.720		2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.090	0.021	0.503
Number of reflections	19388	252	1407
<I/σ(I)>	14.17	38.9	3.3
Completeness [%]	99.9	96.6	100
Redundancy	4.87

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	Internal tracking number 226597. JCSG well D10. 0.1M Cacodylate pH 6.5, 200mM Calcium Acetate, 30.0% w/v PEG400, 20% Ethylene Glycol Cryo. BupsA.00130.a.D227 PD00193 25.2mg/ml., vapor diffusion, sitting drop, temperature 290K