2C1C

Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitors

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MPG/DESY, HAMBURG BEAMLINE BW6
Synchrotron site	MPG/DESY, HAMBURG
Beamline	BW6
Temperature [K]	287
Detector technology	CCD
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	42.012, 58.339, 146.564
Unit cell angles	90.00, 89.87, 90.00

Refinement procedure

Resolution	20.000 - 2.300
R-factor	0.2146
Rwork	0.215
R-free	0.29200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1jqg
RMSD bond length	0.009
RMSD bond angle	1.600
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.440
High resolution limit [Å]	2.300	2.300
Rmerge	0.080
Number of reflections	24576
Completeness [%]	91.4
Redundancy	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1				MES 0.1M PH6,5 AMMONIUM SULPHATE 1,6M DIOXANE 10% YTTRIUM CHLORIDE HEXAHYDRTAE 10MM