6TZ6

Crystal Structure of Candida Albicans Calcineurin A, Calcineurin B, FKBP12 and FK506 (Tacrolimus)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2013-06-27
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9786
Spacegroup name	P 21 21 21
Unit cell lengths	62.470, 142.850, 175.610
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	34.996 - 2.550
R-factor	0.1839
Rwork	0.182
R-free	0.22860
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1tco
RMSD bond length	0.008
RMSD bond angle	0.916
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.620
High resolution limit [Å]	2.550	2.550
Rmerge	0.083	0.560
Rmeas	0.094	0.635
Number of reflections	51429	3787
<I/σ(I)>	16.87	3.4
Completeness [%]	98.4	99.2
Redundancy	4.4	4.5
CC(1/2)	0.998	0.826

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.29	289	CANDIDA ALBICANS VCID8024 [CALCINEURIN A FUSED TO CALCINEURIN B] AND R8065 [FKBP12] IN A SEC PURIFIED COMPLEX MEDIATED BY FK506/TACROLIMUS AT 10.2 MG/ ML AND SUPPLEMENTED WITH 25.6UM R8065 AND 32UM FK506. PROTEIN BUFFER INCLUDES 10MM TRIS PH 7.5, 50 MM NACL, 1.0MM CACL2. THE PROTEIN COMPLEX WAS CRYSTALLIZED AGAINST OPTIMIZATION SCREEN AMP_PROPLEX_A10 (OPT SCREEN BASED ON PROPLEX CONDITION A10) WELL B7: 0.1M TRIS-HCL, 15.91% PEG 2,000 MME, 0.1M POTASSIUM CHLORIDE, AND CRYO-PROTECTED WITH 20% ETHYLENE GLYCOL