1HCX

Choline binding domain of the major autolysin (C-LytA) from Streptococcus pneumoniae

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X31
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X31
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-10-30
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.9840,1.0695,1.0715
Spacegroup name	I 2 2 2
Unit cell lengths	58.049, 118.177, 104.859
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.000 * - 2.600
R-factor	0.218 *
Rwork	0.239
R-free	0.28200 *
Structure solution method	MAD
RMSD bond length	0.007 *
RMSD bond angle	1.200 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SOLVE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000	2.740
High resolution limit [Å]	2.600	2.600
Rmerge	0.049 *	0.266 *
Total number of observations	105081 *
Number of reflections	11378
<I/σ(I)>	18	5.4
Completeness [%]	99.7	100
Redundancy	4.5	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	6.4	295 *	30% PEG 4000, 0.2 M NA-ACETATE, 0.1 M AMMONIUM-ACETATE, PH 6.4, 0.15 M CHOLINE-CL, 0.4 MM DDAO.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	30 (%(w/v))
2	1	reservoir	ammonium acetate	0.2 (M)
3	1	reservoir	sodium citrate	0.1 (M)	pH6.4
4	1	reservoir	DDOA	0.4 (mM)