4HWY

Trypanosoma brucei procathepsin B solved from 40 fs free-electron laser pulse data by serial femtosecond X-ray crystallography

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]	293
Detector technology	PIXEL
Collection date	2011-02-01
Detector	Cornell-SLAC Pixel Array Detector
Wavelength(s)	1.32
Spacegroup name	P 42 21 2
Unit cell lengths	125.400, 125.400, 54.560
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	88.670 - 2.100
R-factor	0.18335
Rwork	0.182
R-free	0.21308
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3mor
RMSD bond length	0.013
RMSD bond angle	1.540
Data reduction software	CrystFEL
Data scaling software	CrystFEL
Phasing software	MOLREP
Refinement software	REFMAC (5.6.0117)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.175
High resolution limit [Å]	2.100	2.100
Number of reflections	25969
Completeness [%]	100.0	100

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Crystallization in vivo within living SF9 insect cells	7.4	310.15	Spontaneous formation of needle-shaped microcrystals in Sf9 cells infected with recombinant baculovirus containing the gene encoding the pre-pro form of Trypanosoma brucei cathepsin B, pH 7.4, Crystallization in vivo within living SF9 insect cells, temperature 310.15K