5TU0

1.9 Angstrom Resolution Crystal Structure of Maltose-Binding Periplasmic Protein MalE from Listeria monocytogenes in Complex with Maltose

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2016-10-27
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 21 21 21
Unit cell lengths	58.208, 78.452, 90.690
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.670 - 1.900
R-factor	0.17603
Rwork	0.174
R-free	0.20823
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2xd3
RMSD bond length	0.009
RMSD bond angle	1.339
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0155)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.081	0.779
Number of reflections	33694
<I/σ(I)>	34.4	2.9
Completeness [%]	100.0	100
Redundancy	7	6.8
CC(1/2)		0.826

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		295	Protein: 15.2 mg/ml, 0.5M Sodium chloride, 0.01M Tris HCl (pH 8.3), 2mM MAL; Screen: Classics II (C2), 1.1M Ammonium tartrate (pH 7.0).