5TRO

1.8 Angstrom Resolution Crystal Structure of Dimerization and Transpeptidase domains (residues 39-608) of Penicillin-Binding Protein 1 from Staphylococcus aureus.

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	2016-10-20
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	C 1 2 1
Unit cell lengths	178.843, 72.202, 86.362
Unit cell angles	90.00, 103.18, 90.00

Refinement procedure

Resolution	29.590 - 1.800
R-factor	0.18088
Rwork	0.179
R-free	0.20946
Structure solution method	SAD
RMSD bond length	0.009
RMSD bond angle	1.365
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHENIX
Refinement software	REFMAC (5.8.0155)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.830
High resolution limit [Å]	1.800	1.800
Rmerge	0.088	0.749
Number of reflections	98204
<I/σ(I)>	26.8	2.3
Completeness [%]	99.7	99.3
Redundancy	5.4	4.9
CC(1/2)		0.793

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.3	295	Protein: 10.8 mg/ml, 0.5M Sodium chloride, 0.01M Tris HCl (pH 8.3), Screen: JCSG+ (A5), 0.2M Magnesium formate, 20% (w/v) PEG 3350.