4ZJ1

Crystal Structure of p-acrylamido-phenylalanine modified TEM1 beta-lactamase from Escherichia coli : V216AcrF mutant

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2014-09-04
Detector	RIGAKU RAXIS HTC
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	45.470, 47.240, 128.330
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 - 1.540
R-factor	0.14185
Rwork	0.140
R-free	0.17045
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1btl
RMSD bond length	0.016
RMSD bond angle	1.851
Data reduction software	iMOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.8.0103)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	26.540	1.630
High resolution limit [Å]	1.540	1.540
Rmerge	0.064	0.188
Number of reflections	41549
<I/σ(I)>	16.3	6.5
Completeness [%]	100.0	100
Redundancy	7.4	7.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.8	295	0.1M 2-(N-morpholino) ethanesulfonic acid (MES) pH 6.5, 15% PEG 20.000 and 15% PEG 550MME