3C1L

Crystal structure of an antioxidant defense protein (mlr4105) from mesorhizobium loti maff303099 at 2.00 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL11-1
Synchrotron site	SSRL
Beamline	BL11-1
Temperature [K]	100
Detector technology	CCD
Collection date	2007-02-11
Detector	MARMOSAIC 325 mm CCD
Wavelength(s)	0.91837
Spacegroup name	P 1 21 1
Unit cell lengths	65.690, 68.060, 266.830
Unit cell angles	90.00, 95.94, 90.00

Refinement procedure

Resolution	29.814 - 2.000
R-factor	0.174
Rwork	0.171
R-free	0.22500
Structure solution method	SAD + MOLECULAR REPLACEMENT
RMSD bond length	0.016
RMSD bond angle	1.498
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	SHARP
Refinement software	REFMAC (5.4.0066)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.814	29.814	2.070
High resolution limit [Å]	2.000	4.300	2.000
Rmerge	0.058	0.028	0.354
Number of reflections	138837	29561	12737
<I/σ(I)>	7.38	16.7	1.6
Completeness [%]	84.6	94.6	41.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	277	NANODROP, 20.0% PEG 6000, 0.1M Tris-HCl pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K
2	VAPOR DIFFUSION, SITTING DROP	6.2	277	NANODROP, 0.2M NaCl, 50.0% PEG 200, 0.1M Na,K Phosphate pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 277K