1BUE

NMC-A CARBAPENEMASE FROM ENTEROBACTER CLOACAE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1996-05-07
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	78.690, 52.900, 67.470
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	31.000 - 1.640
R-factor	0.192
Rwork	0.192
R-free	0.21400
Structure solution method	SIRAS
Starting model (for MR)	NOT APPLICABLE
RMSD bond length	0.006
RMSD bond angle	23.370 *
Data reduction software	MOSFLM
Data scaling software	CCP4
Phasing software	CCP4
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	31.000	1.680
High resolution limit [Å]	1.640	1.640
Rmerge	0.045
Total number of observations	111487 *
Number of reflections	32762
<I/σ(I)>	33.3	7.1
Completeness [%]	93.3	68
Redundancy	4.1	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	5.25	22 *	INITIAL PROTEIN CONCENTRATION WAS 2.0 G/L EQUILIBRATED AGAINST 0.200 M MES PH 5.25, 20% (W/V)PEG 1500, 6% (V/V) N-PROPANOL AT 295K.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2.0 (mg/ml)
2	1	drop	MES	45 (mM)
3	1	drop	PEG1500	5 (%(w/v))
4	1	reservoir	MES	200 (mM)
5	1	reservoir	PEG1500	20 (%(w/v))
6	1	reservoir	n-propyl alcohol	6 (%(v/v))