8FI5
Crystal Structure of Glycylpeptide N-tetradecanoyltransferase (N-myristoyl transferase) (NMT) from Leishmania major Friedlin bound to tetradecanoyl-CoA (Orthorhombic P Form 2)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 19-ID |
Synchrotron site | NSLS-II |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-12-10 |
Detector | DECTRIS EIGER2 XE 9M |
Wavelength(s) | 0.9786 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 59.499, 90.238, 92.523 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.670 - 2.250 |
R-factor | 0.1891 |
Rwork | 0.186 |
R-free | 0.24220 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.140 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.670 | 2.320 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.105 | 1.225 |
Rmeas | 0.112 | 1.303 |
Rpim | 0.037 | 0.438 |
Total number of observations | 221517 | 18921 |
Number of reflections | 24336 | 2184 |
<I/σ(I)> | 12 | 1.9 |
Completeness [%] | 100.0 | |
Redundancy | 9.1 | 8.7 |
CC(1/2) | 0.998 | 0.715 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 291 | 0.1 M Bicine, 20% PEG 6000, LemaA.18219.a.B2.PS38707 at 11.17 mg/mL. Tray: Tray 383B3/1 mM Perez-1, Puck: HR00406_03, Cryo: 20% PEG ethylene glycol. MYA ligand was acquired from the expression host and not added prior to crystallization. |