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Open data
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Basic information
| Entry | Database: PDB / ID: 7yim | ||||||
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| Title | Cryo-EM structure of human Alpha-fetoprotein | ||||||
Components | Alpha-fetoprotein | ||||||
Keywords | METAL BINDING PROTEIN / metal binding / fatty acids binding | ||||||
| Function / homology | Function and homology informationprogesterone metabolic process / ovulation from ovarian follicle / homeostasis of number of cells / Post-translational protein phosphorylation / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / immune response / endoplasmic reticulum lumen / apoptotic process / extracellular space / metal ion binding / cytoplasm Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.6 Å | ||||||
Authors | Liu, N. / Liu, K. / Wu, C. / Liu, Z. / Li, M. / Wang, J. / Wang, H.W. | ||||||
| Funding support | 1items
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Citation | Journal: Nat Methods / Year: 2023Title: Uniform thin ice on ultraflat graphene for high-resolution cryo-EM. Authors: Liming Zheng / Nan Liu / Xiaoyin Gao / Wenqing Zhu / Kun Liu / Cang Wu / Rui Yan / Jincan Zhang / Xin Gao / Yating Yao / Bing Deng / Jie Xu / Ye Lu / Zhongmin Liu / Mengsen Li / Xiaoding Wei ...Authors: Liming Zheng / Nan Liu / Xiaoyin Gao / Wenqing Zhu / Kun Liu / Cang Wu / Rui Yan / Jincan Zhang / Xin Gao / Yating Yao / Bing Deng / Jie Xu / Ye Lu / Zhongmin Liu / Mengsen Li / Xiaoding Wei / Hong-Wei Wang / Hailin Peng / ![]() Abstract: Cryo-electron microscopy (cryo-EM) visualizes the atomic structure of macromolecules that are embedded in vitrified thin ice at their close-to-native state. However, the homogeneity of ice thickness, ...Cryo-electron microscopy (cryo-EM) visualizes the atomic structure of macromolecules that are embedded in vitrified thin ice at their close-to-native state. However, the homogeneity of ice thickness, a key factor to ensure high image quality, is poorly controlled during specimen preparation and has become one of the main challenges for high-resolution cryo-EM. Here we found that the uniformity of thin ice relies on the surface flatness of the supporting film, and developed a method to use ultraflat graphene (UFG) as the support for cryo-EM specimen preparation to achieve better control of vitreous ice thickness. We show that the uniform thin ice on UFG improves the image quality of vitrified specimens. Using such a method we successfully determined the three-dimensional structures of hemoglobin (64 kDa), α-fetoprotein (67 kDa) with no symmetry, and streptavidin (52 kDa) at a resolution of 3.5 Å, 2.6 Å and 2.2 Å, respectively. Furthermore, our results demonstrate the potential of UFG for the fields of cryo-electron tomography and structure-based drug discovery. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7yim.cif.gz | 112.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7yim.ent.gz | 86.6 KB | Display | PDB format |
| PDBx/mmJSON format | 7yim.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7yim_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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| Full document | 7yim_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | 7yim_validation.xml.gz | 25.8 KB | Display | |
| Data in CIF | 7yim_validation.cif.gz | 36.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yi/7yim ftp://data.pdbj.org/pub/pdb/validation_reports/yi/7yim | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 33861MC ![]() 7xgyC ![]() 8gvkC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 68757.406 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AFP, HPAFP / Production host: Homo sapiens (human) / References: UniProt: P02771 |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Alpha-fetoprotein with no symmetry / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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| Molecular weight | Value: 0.067 MDa / Experimental value: YES |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1200 nm / Nominal defocus min: 600 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING ONLY |
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| 3D reconstruction | Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 354264 / Symmetry type: POINT |
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Homo sapiens (human)
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FIELD EMISSION GUN