7KPS
Structure of a GNAT superfamily PA3944 acetyltransferase in complex with AcCoA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-03-09 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.979 |
Spacegroup name | P 1 |
Unit cell lengths | 36.563, 44.246, 60.183 |
Unit cell angles | 97.94, 106.72, 89.92 |
Refinement procedure
Resolution | 37.430 - 1.800 |
R-factor | 0.2078 |
Rwork | 0.206 |
R-free | 0.23540 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6edd |
RMSD bond length | 0.003 |
RMSD bond angle | 1.180 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.830 |
High resolution limit [Å] | 1.800 | 4.880 | 1.800 |
Rmerge | 0.095 | 0.027 | 0.592 |
Rmeas | 0.102 | 0.035 | 0.809 |
Rpim | 0.068 | 0.023 | 0.549 |
Number of reflections | 32365 | 1659 | 1609 |
<I/σ(I)> | 5.5 | ||
Completeness [%] | 97.1 | 98.9 | 95.6 |
Redundancy | 2.2 | 2.2 | 1.9 |
CC(1/2) | 0.985 | 0.553 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.3 uL of 10 mg/mL protein incubated with 5mM AcCoA and 5 mM (R)-3-(2-chloroacetamido)-4-(((S)-1-methoxy-1-oxo-3-phenylpropan-2-yl)amino)-4-oxobutanoic acid was mixed with 0.2 uL of the well condition (MCSG suite I condition 11 - 100 mM Tris-HCl pH 7.0, 200 mM calcium acetate, 20% w/v PEG 3000) and equilibrated against well solution in 96 Well 3 drop Crystallization Plate (Swissci). |