3OTG

Crystal Structure of CalG1, Calicheamicin Glycostyltransferase, TDP bound form

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2009-10-18
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9794, 0.9641
Spacegroup name	P 61 2 2
Unit cell lengths	106.177, 106.177, 155.817
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	45.976 - 2.080
R-factor	0.1943
Rwork	0.193
R-free	0.22700
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	1.005
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	PHENIX (1.6.1_357)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.150
High resolution limit [Å]	2.080	5.720	2.110
Rmerge	0.082	0.042	0.814
Number of reflections	31794
<I/σ(I)>	12.1
Completeness [%]	100.0	99.6	99.7
Redundancy	41.9	38	32.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		298	Protein Solution (20mg/ml CalG1 protein, 20mM Tris pH 8) mixed in a 1:1 ratio with the well solution (20% PEG3350, 0.2M LiSO4, 100mM BisTris pH 6.5) Cryoprotected with 20% ethylene glycol, 20% PEG3350, 0.2M LiSO4, 100mM BisTris pH 6.5, vapor diffusion, hanging drop, temperature 298K, VAPOR DIFFUSION, HANGING DROP