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7F26

Crystal structure of lysozyme

Summary for 7F26
Entry DOI10.2210/pdb7f26/pdb
DescriptorLysozyme C (2 entities in total)
Functional Keywordslysozyme, protein binding
Biological sourceGallus gallus (Chicken)
Total number of polymer chains1
Total formula weight14331.16
Authors
Liang, M. (deposition date: 2021-06-10, release date: 2021-09-15, Last modification date: 2024-10-16)
Primary citationLiang, M.,Yu, L.,Wang, Z.,Zhou, H.,Zhang, Y.,Wang, Q.,He, J.
Novel combined crystallization plate for high-throughput crystal screening and in situ data collection at a crystallography beamline.
Acta Crystallogr.,Sect.F, 77:319-327, 2021
Cited by
PubMed Abstract: In situ microplates are small in size, crystal cultivation and operation are difficult, and the efficiency of crystal screening is relatively low. To solve this problem, a novel combined crystallization plate was designed for high-throughput crystal cultivation and in situ data collection. A frame was used to hold 48 in situ microplates, and the in situ microplates were sealed on one side with an ultralow background-scattering Kapton film. An automatic liquid handler (Mosquito) was used to add a liquid drop to the in situ microplates in the frame, and CrystalClear HD tape was used to seal the frame. A sealed frame holding 48 microplates was developed as a novel combined crystallization plate and was used for crystal cultivation under different conditions and in situ data collection at the synchrotron beamline. Moreover, individual microplates can be separated from the combined crystal plate and then fixed on a magnetic base or loaded onto a UniPuck for in situ data collection. Automatic grid scanning was used to locate crystals. The efficiency of the combined crystallization plate for crystal screening was verified. This method avoids the manual manipulation of crystals during crystal screening and diffraction data collection; therefore, the combined crystallization plate is suitable for large-scale screening of microcrystals.
PubMed: 34473109
DOI: 10.1107/S2053230X21008104
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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