4GF5

Crystal Structure of Calicheamicin Methyltransferase, CalS11

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2011-11-05
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 1
Unit cell lengths	75.112, 106.240, 184.600
Unit cell angles	80.88, 81.65, 70.02

Refinement procedure

Resolution	49.322 - 2.200
R-factor	0.1594
Rwork	0.159
R-free	0.21300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3tos
RMSD bond length	0.007
RMSD bond angle	1.186
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX (1.8_1069)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.240
High resolution limit [Å]	2.200	5.970	2.200
Rmerge	0.110	0.042	0.484
Number of reflections	254196
<I/σ(I)>	6.3
Completeness [%]	94.8	99.7	62.9
Redundancy	3.9	3.9	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	298	Protein solution (11 mg/ml CalS11, 25mM Tris pH 8.0, 5 mg/ml calicheamicin) mixed in a 1:1 ratio with the well solution (25% PEG 3350, .2M LiSO4, .1M Tris pH 8.5) Cryoprotected with 30% PEG 3350, .2M LiSO4, .1M Tris pH 8.5, Vapor diffusion, hanging drop, temperature 298K