4QUS

1.28 Angstrom resolution crystal structure of predicted acyltransferase with acyl-CoA N-acyltransferase domain (ypeA) from Escherichia coli str. K-12 substr. MG1655

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2014-06-04
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97910
Spacegroup name	I 4
Unit cell lengths	90.817, 90.817, 84.167
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.720 - 1.280
R-factor	0.11083
Rwork	0.109
R-free	0.13859
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2pdo
RMSD bond length	0.010
RMSD bond angle	1.643
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.300
High resolution limit [Å]	1.280	1.280
Rmerge	0.052	0.619
Number of reflections	87246
<I/σ(I)>	26.25	2.5
Completeness [%]	99.9	100
Redundancy	5	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	9	295	7 mg/mL protein (no tag) in 10 mM Tris-HCl, pH 8.3, 500 mM sodium chloride, 5 mM BME, crystallization: the PACT Suite A6 (#6): 0.1 M SPG buffer, pH 9.0, 25% w/v PEG1500, cryo-protection: well solution soak, VAPOR DIFFUSION, SITTING DROP, temperature 295K