3TOS

Crystal Structure of CalS11, Calicheamicin Methyltransferase

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	2011-04-26
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9794
Spacegroup name	P 1
Unit cell lengths	78.321, 106.080, 106.330
Unit cell angles	68.69, 69.63, 88.56

Refinement procedure

Resolution	43.101 - 1.550
R-factor	0.1466
Rwork	0.146
R-free	0.17300
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.019
RMSD bond angle	1.716
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	PHENIX (1.6.4_486)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.580
High resolution limit [Å]	1.550	4.210	1.550
Rmerge	0.079	0.057	0.297
Number of reflections	417415
<I/σ(I)>	10
Completeness [%]	96.8	99.2	94.6
Redundancy	3.9	3.8	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		298	Protein Solution (16 mg/ml CalS11 protein, 0.0003M TCEP, 0.05M NaCl, 0.005M HEPES pH 8) mixed in a 1:1 ratio with the well solution(17.6% MEPEG5K, 160mM K-Glutamate, 100mM BisTris pH 6.5)Cryoprotected with 20% Ethylene Glycol, 17.6% MEPEG5K, 160mM KGlutamate, 100mM BisTris pH 6.5, vapor diffusion, hanging drop, temperature 298K, VAPOR DIFFUSION, HANGING DROP