4ABB
Fragments bound to bovine trypsin for the SAMPL challenge
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-08-23 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.509, 58.285, 66.771 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.910 - 1.250 |
R-factor | 0.142 |
Rwork | 0.141 |
R-free | 0.15518 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1k1m |
RMSD bond length | 0.027 |
RMSD bond angle | 2.517 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.900 | 1.320 |
High resolution limit [Å] | 1.250 | 1.250 |
Rmerge | 0.058 | 0.240 |
Number of reflections | 59467 | |
<I/σ(I)> | 21.6 | 7.4 |
Completeness [%] | 99.9 | 99.5 |
Redundancy | 7 | 6.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5.8 | 22.5% PEG 3350, 0.18 M AMMONIUM SULFATE, 0.12 M SODIUM THIOCYANATE, 0.09 M BIS-TRIS PH 5.5, 0.01 M TRIS PH 8.5 (FINAL MEASURED PH=5.82). THE PROTEIN WAS AT 2 MM (47 MG/ML), WITH 4 MM BENZYLAMINE AND 10 MM CALCIUM CHLORIDE ADDED TO STABILIZE IT. THE CRYSTALLIZATIONS WERE SET UP WITH A PHOENITO PROTOCOL (NEWMAN ET AL. 2008), WHERE A PHOENIX ROBOT (ART ROBBINS INSTRUMENTS, SUNNYSIDE, CA) WAS USED TO DISPENSE THE PROTEIN INTO AN SD2 CRYSTALLIZATION PLATE (PRE-FILLED WITH 50 ML RESERVOIR SOLUTION) AND A MOSQUITO ROBOT (TTP LABTECH, MELBOURN, UK) WAS USED TO DISPENSE THE RESERVOIR SOLUTION AND SEED STOCK OVER THE PROTEIN DROPLET. |