4W8J

Structure of the full-length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Detector technology	CCD
Collection date	2011-08-02
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.00
Spacegroup name	P 41 21 2
Unit cell lengths	87.314, 87.314, 266.396
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	82.970 - 2.780
R-factor	0.23173
Rwork	0.226
R-free	0.33226
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	in house
RMSD bond length	0.012
RMSD bond angle	1.399
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	87.000	2.900
High resolution limit [Å]	2.780	2.780
Rmerge	0.096	0.620
Number of reflections	26818
<I/σ(I)>	13.8	2.1
Completeness [%]	99.6	100
Redundancy	4.6	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.84	292	600 nL of 13 mg/mL protein in 20 mM ethanolamine buffer with 0.35 M NaCl was mixed with 600 nL of 700 mM sodium-potassium tartrate, 100 mM BIS-TRIS propane pH 7.84 and 120 nL of 9 mM n-decyl thiomaltoside, and the resulting 1.2 uL sitting drop was allowed to equili- brate against 80uL of the tartrate/BIS-TRIS propane reservoir solution at 19C.