3RUN

New strategy to analyze structures of glycopeptide antibiotic-target complexes

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X6A
Synchrotron site	NSLS
Beamline	X6A
Temperature [K]	93
Collection date	2011-03-25
Wavelength(s)	1.000
Spacegroup name	P 32 2 1
Unit cell lengths	60.440, 60.440, 96.830
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.784 - 1.400
R-factor	0.1491
Rwork	0.147
R-free	0.17990
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2lzm
RMSD bond length	0.008
RMSD bond angle	1.317
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (1.6.2_432)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	19.800		1.440
High resolution limit [Å]	1.400	6.260	1.400
Rmerge	0.076	0.042	0.652
Rmeas		0.047	0.745
Number of reflections	77081	850	5100
<I/σ(I)>	13.75	37.38	2.04
Completeness [%]	98.8	97.1	87.7
Redundancy	5.48

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	291	0.2M ammonium phosphate, 0.1M Tris 8.5, 35% MPD, vapor diffusion, hanging drop, temperature 291K