1IEM

Crystal Structure of AmpC beta-lactamase from E. coli in Complex with a Boronic Acid Inhibitor (1, CefB4)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-07-04
Detector	MARRESEARCH
Wavelength(s)	1.08
Spacegroup name	C 1 2 1
Unit cell lengths	118.560, 78.060, 97.240
Unit cell angles	90.00, 115.44, 90.00

Refinement procedure

Resolution	20.000 - 2.300
R-factor	0.182 *
Rwork	0.182
R-free	0.22800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1fsy
RMSD bond length	0.009
RMSD bond angle	1.510
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.380
High resolution limit [Å]	2.300	2.300
Rmerge	0.075	0.359
Total number of observations	137203 *
Number of reflections	35024 *
<I/σ(I)>	11.2
Completeness [%]	98.8	99.9
Redundancy	3.9

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	drop	potassium phosphate	1.7 (M)
2	1	drop	protein	0.095 (mM)
3	1	reservoir	DMSO	2 (%)
4	1	reservoir	potassium phosphate	1.7 (M)