5E31

2.3 Angstrom Crystal Structure of the Monomeric Form of Penicillin Binding Protein 2 Prime from Enterococcus faecium.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2015-08-24
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	61.440, 64.340, 182.786
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.120 - 2.300
R-factor	0.19925
Rwork	0.197
R-free	0.24445
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5dvy
RMSD bond length	0.011
RMSD bond angle	1.517
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0073)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.120	2.340
High resolution limit [Å]	2.300	2.300
Rmerge	0.131	0.637
Number of reflections	33135
<I/σ(I)>	22.4	3.3
Completeness [%]	99.8	100
Redundancy	7	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	295	Protein: 13.9 mg/ml, 0.5M Sodium chloride, 0.01M Tris-HCL (pH 8.3), 5mM Penicillin V; Screen: Classics II (H7), 0.15M DL-Malic acid (pH 7.0), 20% (w/v) PEG 3350.