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 |
