3I11

Cobalt-substituted metallo-beta-lactamase from Bacillus cereus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2008-06-06
Detector	MAR scanner 345 mm plate
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	53.087, 61.363, 69.570
Unit cell angles	90.00, 93.00, 90.00

Refinement procedure

Resolution	40.130 - 1.450
R-factor	0.164
Rwork	0.162
R-free	0.20400
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.021
RMSD bond angle	1.782
Data reduction software	MOSFLM
Data scaling software	SCALA (3.2.25)
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.129	40.130	1.530
High resolution limit [Å]	1.450	4.590	1.450
Rmerge	0.057	0.044	0.374
Total number of observations		7674	12600
Number of reflections	35794
<I/σ(I)>	7.418	12.7	2
Completeness [%]	90.8	99.5	84.4
Redundancy	3.5	6	2.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.8	293	0.1 M Sodium cacodylate, 0.1 M Sodium tartrate, 18% PEG 3350. Crystals of the apo-protein were soaked in 1 mM CoSO4, pH 5.8, Vapor diffusion, hanging drop, temperature 293K