1DY6

Structure of the imipenem-hydrolyzing beta-lactamase SME-1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	291
Detector technology	DIFFRACTOMETER
Detector	ENRAF-NONIUS FAST
Spacegroup name	P 1 21 1
Unit cell lengths	81.500, 51.720, 71.690
Unit cell angles	90.00, 118.62, 90.00

Refinement procedure

Resolution	10.000 - 2.130
R-factor	0.184
Rwork	0.184
R-free	0.24400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	MODIFIED NMC-A BETA-LACTAMASE (1BUE) SOFTWARE USED: AMORE
RMSD bond length	0.007
RMSD bond angle	1.440
Data reduction software	MADNESS
Data scaling software	Agrovata
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.130	2.130 *
Rmerge	0.049 *	0.216 *
Total number of observations	55772 *
Number of reflections	24447	1601 *
Completeness [%]	82.0	30.1 *
Redundancy	2.3	2.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5		PROTEIN WAS CRYSTALLIZED FROM 17% PEG 4000, 0.2 M AMMONIUM ACETATE, 0.1 M TRIS-HCL, PH 8.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	17 (%)
2	1	reservoir	ammonium acetate	0.2 (M)
3	1	reservoir	Tris-HCl	0.1 (M)