5CFA

Crystal structures of Bbp from Staphylococcus aureus with peptide ligand

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL17U
Synchrotron site	SSRF
Beamline	BL17U
Temperature [K]	100
Detector technology	CCD
Collection date	2014-06-28
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.979
Spacegroup name	P 1 21 1
Unit cell lengths	60.916, 74.961, 75.563
Unit cell angles	90.00, 102.91, 90.00

Refinement procedure

Resolution	36.560 - 1.450
R-factor	0.18
Rwork	0.178
R-free	0.21220
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5cf3
RMSD bond length	0.007
RMSD bond angle	1.140
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.500
High resolution limit [Å]	1.450	3.120	1.450
Rmerge	0.084	0.051	0.865
Rmeas	0.093	0.057	0.976
Rpim	0.041	0.025	0.442
Total number of observations	591166
Number of reflections	116230
<I/σ(I)>	6.9
Completeness [%]	99.2	99.6	95.8
Redundancy	5.1	5.3	4.5
CC(1/2)		0.997	0.747

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		291.15	peptide was added into the concentrated protein samples at 10:1 ratio and the protein-peptide complex crystals are grown in 0.2 M lithium sulfate, 0.1M Tris-HCl pH8.2, 30% PEG4000 protein concentration was 30mg/ml