3LST

Crystal Structure of CalO1, Methyltransferase in Calicheamicin Biosynthesis, SAH 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	2009-07-06
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9794, 0.9641
Spacegroup name	C 2 2 21
Unit cell lengths	63.515, 93.603, 240.971
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.174 - 2.400
R-factor	0.203
Rwork	0.200
R-free	0.25100
Structure solution method	MAD
RMSD bond length	0.004
RMSD bond angle	0.717
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	PHENIX (1.5_2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.440
High resolution limit [Å]	2.400	2.400
Rmerge	0.120	0.525
Number of reflections	28057
<I/σ(I)>	9.7
Completeness [%]	97.7	83.4
Redundancy	12.3	9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	298	Protein Solution 20mg/ml CalO1 protein, 20mM Tris pH 8, mixed in a 1:1 ratio with the well solution 20% MEPEG 5K, 0.2M Glycine, 0.1M BTP pH 7.0. Cryoprotected with 20% ethylene glycol, 20% MEPEG 5K, 0.2M Glycine, 0.1M BTP pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K