4OW3

Thermolysin structure determined by free-electron laser

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	FREE ELECTRON LASER
Source details	SLAC LCLS BEAMLINE CXI
Synchrotron site	SLAC LCLS
Beamline	CXI
Temperature [K]	298
Detector technology	PIXEL
Collection date	2011-12-01
Detector	CS-PAD detector
Wavelength(s)	1.269, 1.297
Spacegroup name	P 61 2 2
Unit cell lengths	92.893, 92.893, 130.438
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	68.472 - 2.100
R-factor	0.219654161884
Rwork	0.217
R-free	0.26317
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2tli
RMSD bond length	0.003
RMSD bond angle	0.682
Refinement software	PHENIX ((phenix.refine: dev_1549+SVN))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	68.500	2.180
High resolution limit [Å]	2.100	2.100
Number of reflections	19861
<I/σ(I)>	50.2	5.6
Completeness [%]	99.1	91.2
Redundancy	209	4.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION	6.5	298	300 ul of the protein stock was mixed in a 1:1 ratio with 40% PEG 2000, 100 mM MES pH 6.5, 5 mM CaCl2. Crystallization occurred within minutes.