4WHN

Structure of toxin-activating acyltransferase (TAAT)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	CCD
Collection date	2012-03-02
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9796
Spacegroup name	P 21 21 21
Unit cell lengths	82.450, 86.370, 131.160
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	54.290 - 2.150
R-factor	0.20228
Rwork	0.200
R-free	0.24238
Structure solution method	SAD
RMSD bond length	0.016
RMSD bond angle	1.714
Data reduction software	iMOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.8.0073)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	54.290	2.220
High resolution limit [Å]	2.150	2.150
Rmerge		0.804
Number of reflections	51711
<I/σ(I)>	12.6	2.5
Completeness [%]	100.0	100
Redundancy	7.2	7.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.4	288	Crystallisation reagent is 32% PEG300, Phosphate-citrate buffer, pH 4.4. Protein solution is 5 mg/ml ApxC in 150mM NaCl, 20 mM HEPES pH 7.5. Sitting drops formed by 2 ul Protein solution and 1 ul crystallisation reagent equilibrated over 80 ul of the reagent alone.