3IAA

Crystal Structure of CalG2, Calicheamicin Glycosyltransferase, TDP bound form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
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	2009-04-07
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97957
Spacegroup name	P 1 21 1
Unit cell lengths	88.787, 48.539, 107.565
Unit cell angles	90.00, 101.79, 90.00

Refinement procedure

Resolution	49.761 - 2.505
R-factor	0.188
Rwork	0.184
R-free	0.23800
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	0.906
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.540
High resolution limit [Å]	2.500	6.780	2.500
Rmerge	0.162	0.054	0.493
Number of reflections	30322
<I/σ(I)>	5.7
Completeness [%]	96.2	99.9	81.3
Redundancy	6.1	6.2	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		298	Protein Solution (20 mg/ml CalG4 Protein, 0.05 M NaCl, 0.015 M Tris pH 8) mixed in a 1:1 ratio with the Well Solution (0.8M Na3Citrate, 0.1M BisTris pH 6.5) Cryoprotected with 20% ethylene glycol, 0.8M Na3Citrate, 0.1M BisTris pH 6.5, vapor diffusion, hanging drop, temperature 298K