2PCU

Human carboxypeptidase A4 in complex with a cleaved hexapeptide.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	110
Detector technology	CCD
Collection date	2006-01-01
Detector	ADSC QUANTUM 210
Wavelength(s)	1.036
Spacegroup name	P 21 21 21
Unit cell lengths	50.304, 72.494, 81.575
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.600
R-factor	0.159
Rwork	0.159
R-free	0.17600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2bo9
RMSD bond length	0.017
RMSD bond angle	1.626
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	72.548	1.690
High resolution limit [Å]	1.600	1.600
Rmerge	0.093	0.346
Total number of observations		17578
Number of reflections	39536
<I/σ(I)>	4.1	2
Completeness [%]	98.7	95.1
Redundancy	6.1	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	277	Crystals were obtained from sitting drops subjected to vapor diffusion and containing consisting of 100nL of hCPA4:hexapeptide (15 mg/mL in 5mM Tris HCl pH 7.5) and 100nL of reservoir solution (0.2M potassium thiocyanate / 20% PEG 3350). Crystallisation drops were dispensed on 96x3-well Greiner plates by a Tecan robot and a Cartesian nanodrop robot (Genomic Solutions) at the joint IBMB-CSIC/Barcelona Science Park Automated Crystallization Platform (PAC). Crystals appeared after incubation for 10-15 days in a Bruker steady-temperature crystal farm at 4 C., VAPOR DIFFUSION, SITTING DROP, temperature 277K