5VNQ
Neutron crystallographic structure of perdeuterated T4 lysozyme cysteine-free pseudo-wild type at cryogenic temperature
Summary for 5VNQ
| Entry DOI | 10.2210/pdb5vnq/pdb |
| Related | 5VNR |
| Descriptor | Endolysin, CHLORIDE ION (3 entities in total) |
| Functional Keywords | t4 lysozyme, neutron crystallography, hydrogen bonding network, hydrogen bond, water, hydrolase |
| Biological source | Enterobacteria phage T4 |
| Total number of polymer chains | 1 |
| Total formula weight | 18699.27 |
| Authors | Li, L.,Shukla, S.,Meilleur, F.,Standaert, R.F.,Pierce, J.,Myles, D.A.A.,Cuneo, M.J. (deposition date: 2017-05-01, release date: 2017-07-26, Last modification date: 2023-10-04) |
| Primary citation | Li, L.,Shukla, S.,Meilleur, F.,Standaert, R.F.,Pierce, J.,Myles, D.A.A.,Cuneo, M.J. Neutron crystallographic studies of T4 lysozyme at cryogenic temperature. Protein Sci., 26:2098-2104, 2017 Cited by PubMed Abstract: Bacteriophage T4 lysozyme (T4L) has been used as a paradigm for seminal biophysical studies on protein structure, dynamics, and stability. Approximately 700 mutants of this protein and their respective complexes have been characterized by X-ray crystallography; however, despite the high resolution diffraction limits attained in several studies, no hydrogen atoms were reported being visualized in the electron density maps. To address this, a 2.2 Å-resolution neutron data set was collected at 80 K from a crystal of perdeuterated T4L pseudo-wild type. We describe a near complete atomic structure of T4L, which includes the positions of 1737 hydrogen atoms determined by neutron crystallography. The cryogenic neutron model reveals explicit detail of the hydrogen bonding interactions in the protein, in addition to the protonation states of several important residues. PubMed: 28707382DOI: 10.1002/pro.3231 PDB entries with the same primary citation |
| Experimental method | NEUTRON DIFFRACTION (2.2 Å) |
Structure validation
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