3QJ3

Structure of digestive procathepsin L2 proteinase from Tenebrio molitor larval midgut

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LNLS BEAMLINE W01B-MX2
Synchrotron site	LNLS
Beamline	W01B-MX2
Temperature [K]	100
Detector technology	CCD
Collection date	2009-03-30
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.46
Spacegroup name	P 1
Unit cell lengths	51.669, 52.370, 59.716
Unit cell angles	91.28, 91.55, 109.59

Refinement procedure

Resolution	34.560 - 1.850
R-factor	0.1856
Rwork	0.183
R-free	0.23149
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3qt4
RMSD bond length	0.009
RMSD bond angle	1.081
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.000	1.920
High resolution limit [Å]	1.850	1.850
Rmerge	0.054	0.318
Number of reflections	44108
<I/σ(I)>	18.2	2.5
Completeness [%]	87.7	10
Redundancy	3.8	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.7	289	pCAL2Cys25Ser (10 mg/ml), 0.2 M sodium acetate, 0.1 M sodium cacodylate, 20% PEG 8000, pH 6.7, VAPOR DIFFUSION, SITTING DROP, temperature 289K