8FI6
Crystal Structure of Glycylpeptide N-tetradecanoyltransferase (N-myristoyl transferase) (NMT) from Leishmania major Friedlin bound to tetradecanoyl-CoA (Orthorhombic P Form 3)
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 | 55.809, 88.620, 92.490 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.220 - 1.800 |
R-factor | 0.1671 |
Rwork | 0.165 |
R-free | 0.21120 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.017 |
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] | 47.780 | 1.840 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.080 | 1.323 |
Rmeas | 0.085 | 1.399 |
Rpim | 0.028 | 0.447 |
Total number of observations | 393008 | 24005 |
Number of reflections | 43124 | 2515 |
<I/σ(I)> | 14.9 | 1.9 |
Completeness [%] | 99.7 | |
Redundancy | 9.1 | 9.5 |
CC(1/2) | 0.998 | 0.650 |
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% MPD. MYA ligand was acquired from the expression host and not added prior to crystallization. |