3E7D

Crystal Structure of Precorrin-8X Methyl Mutase CbiC/CobH from Brucella melitensis

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	2008-08-01
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97934
Spacegroup name	P 1 21 1
Unit cell lengths	57.724, 68.927, 103.196
Unit cell angles	90.00, 95.88, 90.00

Refinement procedure

Resolution	50.000 - 1.800
R-factor	0.234
Rwork	0.232
R-free	0.26000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1f2v
RMSD bond length	0.010
RMSD bond angle	1.318
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (refmac_5.4.0067)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.136	0.501
Number of reflections	67776
<I/σ(I)>	21.7	2.2
Completeness [%]	91.7	86.8
Redundancy	3	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	289	JCSG+ condition A2, 20% PEG3000, 0.1 M Na citrate pH 5.5, 0.4/0.4 uL drops, Crystal ID 10993a2, 20 mg/mL protein in 20 mM HEPES pH 7.0, 0.3 M NaCl, 5% glycerol, 2 mM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 289K