1FCN

Crystal Structure of the E. Coli AMPC Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Substrate Beta-Lactam LORACARBEF

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Temperature [K]	129
Spacegroup name	C 1 2 1
Unit cell lengths	119.360, 76.264, 98.355
Unit cell angles	90.00, 116.00, 90.00

Refinement procedure

Resolution	8.000 - 2.350
Rwork	0.208
R-free	0.25700
RMSD bond length	0.016 *
RMSD bond angle	1.900 *
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000
High resolution limit [Å]	2.350
Rmerge	0.081	0.227 *
Number of reflections	33137
<I/σ(I)>	11.9
Completeness [%]	95.0 *	94.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.7	23 *	1.7 M potassium phosphate, pH 8.7, VAPOR DIFFUSION, HANGING DROP, temperature 296K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	potassium phosphate	1.7 (M)
2	1	drop	protein	0.1 (mM)