5HNC
Synchrotron X-ray single crystal diffraction from protein microcrystals via magnetically oriented microcrystal arrays in gels
Summary for 5HNC
| Entry DOI | 10.2210/pdb5hnc/pdb |
| Related | 5HNC |
| Descriptor | Lysozyme C (2 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 14331.16 |
| Authors | Tsukui, S.,Kimura, F.,Kusaka, K.,Baba, S.,Mizuno, N.,Kimura, T. (deposition date: 2016-01-18, release date: 2016-07-20, Last modification date: 2024-10-30) |
| Primary citation | Tsukui, S.,Kimura, F.,Kusaka, K.,Baba, S.,Mizuno, N.,Kimura, T. Neutron and X-ray single-crystal diffraction from protein microcrystals via magnetically oriented microcrystal arrays in gels. Acta Crystallogr D Struct Biol, 72:823-829, 2016 Cited by PubMed Abstract: Protein microcrystals magnetically aligned in D2O hydrogels were subjected to neutron diffraction measurements, and reflections were observed for the first time to a resolution of 3.4 Å from lysozyme microcrystals (∼10 × 10 × 50 µm). This result demonstrated the possibility that magnetically oriented microcrystals consolidated in D2O gels may provide a promising means to obtain single-crystal neutron diffraction from proteins that do not crystallize at the sizes required for neutron diffraction structure determination. In addition, lysozyme microcrystals aligned in H2O hydrogels allowed structure determination at a resolution of 1.76 Å at room temperature by X-ray diffraction. The use of gels has advantages since the microcrystals are measured under hydrated conditions. PubMed: 27377379DOI: 10.1107/S2059798316007415 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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