7KH5
Hen Egg White Lysozyme in complex with tetrabromoterephthalic acid
Summary for 7KH5
| Entry DOI | 10.2210/pdb7kh5/pdb |
| Descriptor | Lysozyme C, 2,3,5,6-tetrabromobenzene-1,4-dicarboxylic acid (3 entities in total) |
| Functional Keywords | lyzozyme, hydrolase, antimicrobial protein |
| Biological source | Gallus gallus (Chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 14812.88 |
| Authors | Truong, J.,Nguyen, S. (deposition date: 2020-10-20, release date: 2021-04-28, Last modification date: 2024-11-06) |
| Primary citation | Truong, J.Q.,Nguyen, S.,Bruning, J.B.,Shearwin, K.E. Simplified heavy-atom derivatization of protein structures via co-crystallization with the MAD tetragon tetrabromoterephthalic acid. Acta Crystallogr.,Sect.F, 77:156-162, 2021 Cited by PubMed Abstract: The phase problem is a persistent bottleneck that impedes the structure-determination pipeline and must be solved to obtain atomic resolution crystal structures of macromolecules. Although molecular replacement has become the predominant method of solving the phase problem, many scenarios still exist in which experimental phasing is needed. Here, a proof-of-concept study is presented that shows the efficacy of using tetrabromoterephthalic acid (B4C) as an experimental phasing compound. Incorporating B4C into the crystal lattice using co-crystallization, the crystal structure of hen egg-white lysozyme was solved using MAD phasing. The strong anomalous signal generated by its four Br atoms coupled with its compatibility with commonly used crystallization reagents render B4C an effective experimental phasing compound that can be used to overcome the phase problem. PubMed: 33949976DOI: 10.1107/S2053230X21004052 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.295 Å) |
Structure validation
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