2O3L

Crystal structure of a duf1048 protein with a left-handed superhelix fold (bce_3448) from bacillus cereus atcc 10987 at 2.05 A resolution

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	2006-10-19
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97921, 0.97942, 0.94645
Spacegroup name	P 32 2 1
Unit cell lengths	61.202, 61.202, 101.702
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.298 - 2.050
R-factor	0.186
Rwork	0.184
R-free	0.22700
Structure solution method	MAD
RMSD bond length	0.018
RMSD bond angle	1.501
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SHELX
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.298	29.300	2.100
High resolution limit [Å]	1.999	9.170	2.050
Rmerge	0.071	0.041	0.635
Total number of observations		792	5308
Number of reflections	14352
<I/σ(I)>	6.4	9.5	1.1
Completeness [%]	99.8	96.2	99.3
Redundancy	5.2	4.2	5.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP, NANODROP	6	277	0.8M (NH4)2SO4, 0.1M MES pH 6.0, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K