1I2W

BETA-LACTAMASE FROM BACILLUS LICHENIFORMIS BS3 COMPLEXED WITH CEFOXITIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE D41A
Synchrotron site	LURE
Beamline	D41A
Temperature [K]	288
Detector technology	IMAGE PLATE
Collection date	1998-10-22
Detector	MARRESEARCH
Wavelength(s)	1.375
Spacegroup name	P 1 21 1
Unit cell lengths	47.344, 106.372, 63.873
Unit cell angles	90.00, 94.18, 90.00

Refinement procedure

Resolution	8.000 - 1.700
R-factor	0.216
Rwork	0.216
R-free	0.25600
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	25.400 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA)
Phasing software	AMoRE
Refinement software	X-PLOR ((ONLINE) 3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	22.030 *	1.700
High resolution limit [Å]	1.650 *	1.650 *
Rmerge	0.072 *	0.430 *
Total number of observations	143995 *
Number of reflections	68766	26718 *
<I/σ(I)>	5.4
Completeness [%]	91.8	87.1 *
Redundancy	2.1	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	20 *	PEG 6000, sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG6000	25 (%)
3	1	reservoir	sodium acetate	100 (mM)	pH5.0