3OTH

Crystal Structure of CalG1, Calicheamicin Glycostyltransferase, TDP and calicheamicin alpha3I 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	2010-07-09
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9794
Spacegroup name	P 21 21 21
Unit cell lengths	45.809, 100.100, 169.881
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.121 - 2.301
R-factor	0.1968
Rwork	0.194
R-free	0.24660
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.955
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHENIX (Phaser)
Refinement software	PHENIX (1.6.1_357)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.340
High resolution limit [Å]	2.300	6.240	2.300
Rmerge	0.126	0.089	0.313
Number of reflections	34067
<I/σ(I)>	6
Completeness [%]	95.9	99.9	74.7
Redundancy	6.6	6.6	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	298	Protein Solution (20mg/ml CalG1 protein, 20mM Tris pH 8, 25mM TDP) mixed in a 1:1 ratio with the well solution (16% MEPEG5K, 160mM CaCl2, 100mM MES/Acetate pH 5.5) Cryoprotected with 20% Glycerol, 24% MEPEG5K, 160mM CaCl2, 100mM MES/Acetate pH 5.5, vapor diffusion, hanging drop, temperature 298K, VAPOR DIFFUSION, HANGING DROP