1IEL

Crystal Structure of AmpC beta-lactamase from E. coli in Complex with Ceftazidime

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	2000-07-01
Detector	MARRESEARCH
Wavelength(s)	1.08
Spacegroup name	C 1 2 1
Unit cell lengths	118.490, 77.040, 98.070
Unit cell angles	90.00, 115.76, 90.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.182 *
Rwork	0.182
R-free	0.22600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1fsy
RMSD bond length	0.011
RMSD bond angle	1.600
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	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.058	0.238
Total number of observations	152381 *
Number of reflections	46338 *
<I/σ(I)>	14.8
Completeness [%]	86.5	99.9
Redundancy	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.7	296	used microseeding, Usher, K.C., (1998) Biochemistry, 37, 16082. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium potassium phosphate	1.7 (M)
2	1	drop	protein	10 (mg/ml)