3OTI

Crystal Structure of CalG3, Calicheamicin Glycostyltransferase, TDP and calicheamicin T0 bound form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2010-08-20
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9794
Spacegroup name	P 1 21 1
Unit cell lengths	45.567, 135.090, 62.093
Unit cell angles	90.00, 95.75, 90.00

Refinement procedure

Resolution	29.234 - 1.597
R-factor	0.1528
Rwork	0.152
R-free	0.18060
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	1.557
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER (2.2.4)
Refinement software	PHENIX (1.6.1_357)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.630
High resolution limit [Å]	1.597	4.340	1.600
Rmerge	0.095	0.065	0.388
Number of reflections	96516
<I/σ(I)>	10.8
Completeness [%]	98.0	99.4	84.8
Redundancy	7.1	7.5	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.5	298	Protein Solution (10mg/ml CalG3 protein, 10mM Tris pH 7.5, 50mM NaCl, 25mM TDP, calicheamicin T0) mixed in a 1:1 ratio with the well solution (28% MEPEG2K, 160mM Na3Citrate, 100mM NaAcetate pH 4.5) Cryoprotected with 20% Ethylene Glycol, 28% MEPEG2K, 160mM Na3Citrate, 100mM NaAcetate pH 4.5, vapor diffusion, hanging drop, temperature 298K, VAPOR DIFFUSION, HANGING DROP