2ZJ9

X-ray crystal structure of AmpC beta-Lactamase (AmpC(D)) from an Escherichia coli with a Tripeptide Deletion (Gly286 Ser287 Asp288) on the H10 Helix

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL41XU
Synchrotron site	SPring-8
Beamline	BL41XU
Temperature [K]	100
Detector technology	CCD
Collection date	2006-11-14
Detector	ADSC QUANTUM 315
Wavelength(s)	1.07158
Spacegroup name	P 1
Unit cell lengths	47.065, 47.381, 81.461
Unit cell angles	82.62, 80.91, 65.40

Refinement procedure

Resolution	39.160 - 1.700
R-factor	0.16527
Rwork	0.163
R-free	0.20557
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2bls
RMSD bond length	0.012
RMSD bond angle	1.400
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	AMoRE
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.062	0.267
Total number of observations	141726
Number of reflections	65343
<I/σ(I)>	18.1	2.6
Redundancy	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	293	10mM Hepes, 20% PEG 4000, 5% iso-propanol, 0.05M sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP	5.6	293	10mM Hepes, 20% PEG 4000, 5% iso-propanol, 0.05M sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K