1R77

Crystal structure of the cell wall targeting domain of peptidylglycan hydrolase ALE-1

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2001-06-30
Detector	MARRESEARCH
Wavelength(s)	0.97931, 0.97917, 0.95370
Spacegroup name	P 21 21 21
Unit cell lengths	45.199, 58.521, 85.081
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	17.500 - 1.750
R-factor	0.202
Rwork	0.202
R-free	0.23200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	N-terminus truncated SeMet MAD structure
RMSD bond length	0.006
RMSD bond angle	1.200
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.810
High resolution limit [Å]	1.750	1.750
Number of reflections	22012
Completeness [%]	93.9	98.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	297	PEG 3350, sodium acetate, MES pH 6.5 or HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K
1	VAPOR DIFFUSION, HANGING DROP	6.5	297	PEG 3350, sodium acetate, MES pH 6.5 or HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K