4ES9

Crystal Structure of the adhesin domain of Epf from Streptococcus pyogenes in P21

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	100
Detector technology	CCD
Collection date	2001-03-11
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.979420
Spacegroup name	P 1 21 1
Unit cell lengths	71.080, 117.134, 73.036
Unit cell angles	90.00, 106.46, 90.00

Refinement procedure

Resolution	19.730 - 2.000
R-factor	0.1742
Rwork	0.172
R-free	0.21480
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4es8
RMSD bond length	0.010
RMSD bond angle	1.130
Data reduction software	XDS
Data scaling software	SCALA (3.3.16)
Phasing software	PHASER (2.1.4)
Refinement software	BUSTER-TNT

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	70.042	19.727	2.110
High resolution limit [Å]	2.000	6.320	2.000
Rmerge		0.044	0.441
Total number of observations		8999	41558
Number of reflections	76117
<I/σ(I)>	6.4	14.8	1.7
Completeness [%]	98.4	95.7	99.2
Redundancy	3.7	3.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	291	23 % (w/v) PEG3350, 200 mM K Acetate, pH 7.4, 0.02 MG/ML CHYMOTRYPSIN (Type VII, TLCK-treated, Sigma-Aldrich), temperature 291K, VAPOR DIFFUSION, HANGING DROP