5TR7

Crystal structure of a putative D-alanyl-D-alanine carboxypeptidase from Vibrio cholerae O1 biovar eltor str. N16961

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	2016-10-05
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 31
Unit cell lengths	88.749, 88.749, 85.425
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.050
R-factor	0.19321
Rwork	0.191
R-free	0.23774
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1nzo
RMSD bond length	0.018
RMSD bond angle	2.028
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	BALBES
Refinement software	REFMAC (5.8.0155)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.090
High resolution limit [Å]	2.050	2.050
Rmerge	0.066	0.750
Number of reflections	47191
<I/σ(I)>	36.6	3.1
Completeness [%]	100.0	100
Redundancy	5.8	5.7
CC(1/2)	0.970

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	294	0.2 M Sodium Nitrate, 0.1 M Bis-Tris propane, 20% PEG3350