3FJU

Ascaris suum carboxypeptidase inhibitor in complex with human carboxypeptidase A1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	CCD
Collection date	2008-07-18
Detector	ADSC QUANTUM 315
Wavelength(s)	1.0000
Spacegroup name	P 21 21 21
Unit cell lengths	55.470, 78.700, 84.500
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.370 - 1.600
R-factor	0.15769
Rwork	0.157
R-free	0.20025
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2v77
RMSD bond length	0.011
RMSD bond angle	1.297
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC (5.5.0046)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.400	1.690
High resolution limit [Å]	1.600	1.600
Rmerge	0.086	0.499
Number of reflections	49284
<I/σ(I)>	18.8	4.6
Completeness [%]	99.6	97.7
Redundancy	7.2	7.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	Reservoir solutions were prepared by a Tecan robot and 200-nL crystallization drops were dispensed on 96x3-well CrystalQuick plates (Greiner) by a Cartesian nanodrop robot (Genomic Solutions) at the joint IBMB-CSIC/IRB/Barcelona Science Park High-Throughput Crystallography Platform (PAC). Best crystals appeared after 2-3 weeks in a Bruker steady-temperature crystal farm at 20 C with 0.2 M zinc acetate dihydrate, 0.1 M sodium cacodylate, 9% PEG 8000, pH 6.5 as reservoir solution. These conditions were successfully scaled up to the microliter range with Cryschem crystallization dishes (Hampton Research) using drops containing 3 microl of protein solution (16.5 mg/ml) and 1 microl of reservoir solution, VAPOR DIFFUSION, SITTING DROP, temperature 293K