2P1A

Crystal structure of a putative metal-binding protein (bce_2162) from bacillus cereus atcc 10987 at 2.10 A resolution

Experimental procedure

Experimental method	MAD
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)	0.91162, 0.97904, 0.97926
Spacegroup name	P 21 21 21
Unit cell lengths	45.470, 77.820, 87.070
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.566 - 2.100
R-factor	0.223
Rwork	0.221
R-free	0.26800
Structure solution method	MAD
RMSD bond length	0.014
RMSD bond angle	1.466
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	SHELX
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.566	29.570	2.190
High resolution limit [Å]	2.100	4.530	2.100
Rmerge	0.049	0.030	0.306
Number of reflections	18527
<I/σ(I)>	9.23	22.6	2.45
Completeness [%]	99.1	97.2	97.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	9.5	277	NANODROP, 30.0% PEG 400, 0.1M CHES pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K