1KE3

X-ray crystal structure of AmpC beta-lactamase from E. coli in complex with the inhibitor 4,4'-biphenyldiboronic acid

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	103
Detector technology	IMAGE PLATE
Collection date	1999-03-31
Detector	RIGAKU RAXIS IIC
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	117.800, 78.360, 97.380
Unit cell angles	90.00, 115.93, 90.00

Refinement procedure

Resolution	20.000 - 2.150
Rwork	0.193
R-free	0.23700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1c3b
RMSD bond length	0.010
RMSD bond angle	1.600
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.210
High resolution limit [Å]	2.150	2.150
Rmerge	0.075	0.332
Total number of observations	115882 *
Number of reflections	42306
<I/σ(I)>	15.2	3.7
Completeness [%]	97.7	96.3
Redundancy	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.7	23 *	used microseeding *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	potassium phosphate	1.7 (M)	pH8.7
2	1	drop	protein	0.590 (mM)
3	1	drop	DMSO	2 (%)
4	1	drop	potassium phosphate	1.7 (M)	pH8.7