[English] 日本語

- EMDB-45848: Focused map of the ligase IV catalytic domain in the ligation com... -
+
Open data
-
Basic information
Entry | ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Focused map of the ligase IV catalytic domain in the ligation complex in the NHEJ pathway | |||||||||
![]() | Focused map of ligase IV catalytic domain in the ligation complex I | |||||||||
![]() |
| |||||||||
![]() | NHEJ / ligation / XLF / PAXX / DNA repair / Ligase IV / DNA BINDING PROTEIN | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Li J / Liu L / Gellert M / Yang W | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: The ligation complex in the NHEJ pathway Authors: Li J / Liu L / Gellert M / Yang W | |||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 255.4 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 17.9 KB 17.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 18.2 KB | Display | ![]() |
Images | ![]() | 68.2 KB | ||
Masks | ![]() | 512 MB | ![]() | |
Filedesc metadata | ![]() | 5.6 KB | ||
Others | ![]() ![]() | 474.5 MB 474.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | C: citing same article ( |
---|
-
Links
EMDB pages | ![]() ![]() |
---|
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Focused map of ligase IV catalytic domain in the ligation complex I | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.833 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Mask #1
File | ![]() | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: half 1 map
File | emd_45848_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | half 1 map | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: half 2 map
File | emd_45848_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | half 2 map | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
-Entire : Ligation complex in the NHEJ pathway
Entire | Name: Ligation complex in the NHEJ pathway |
---|---|
Components |
|
-Supramolecule #1: Ligation complex in the NHEJ pathway
Supramolecule | Name: Ligation complex in the NHEJ pathway / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 854 KDa |
-Macromolecule #1: human ligase IV
Macromolecule | Name: human ligase IV / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() |
Sequence | String: GPVMAASQTS QTVASHVPFA DLCSTLERIQ KSKGRAEKIR HFREFLDSWR KFHDALHKNH KDV TDSFYP AMRLILPQLE RERMAYGIKE TMLAKLYIEL LNLPRDGKDA LKLLNYRTPT GTHGDAGDFA MIAYFVLKPR CLQKGSLTIQ QVNDLLDSIA SNNSAKRKDL ...String: GPVMAASQTS QTVASHVPFA DLCSTLERIQ KSKGRAEKIR HFREFLDSWR KFHDALHKNH KDV TDSFYP AMRLILPQLE RERMAYGIKE TMLAKLYIEL LNLPRDGKDA LKLLNYRTPT GTHGDAGDFA MIAYFVLKPR CLQKGSLTIQ QVNDLLDSIA SNNSAKRKDL IKKSLLQLIT QSSALEQKWL IRMIIKDLKL GVSQQTIFSV FHNDAAELHN VTTDLEKVCR QLHDPSVGLS DISI TLFSA FKPMLAAIAD IEHIEKDMKH QSFYIETKLD GERMQMHKDG DVYKYFSRNG YNYTD QFGA SPTEGSLTPF IHNAFKADIQ ICILDGEMMA YNPNTQTFMQ KGTKFDIKRM VEDSDL QTC YCVFDVLMVN NKKLGHETLR KRYEILSSIF TPIPGRIEIV QKTQAHTKNE VIDALNE AI DKREEGIMVK QPLSIYKPDK RGEGWLKIKP EYVSGLMDEL DILIVGGYWG KGSRGGMM S HFLCAVAEKP PPGEKPSVFH TLSRVGSGCT MKELYDLGLK LAKYWKPFHR KAPPSSILC GTEKPEVYIE PCNSVIVQIK AAEIVPSDMY KTGCTLRFPR IEKIRDDKEW HECMTLDDLE QLRGKASGK LASKHLYIGG DDEPQEKKRK AAPKMKKVIG IIEHLKAPNL TNVNKISNIF E DVEFCVMS GTDSQPKPDL ENRIAEFGGY IVQNPGPDTY CVIAGSENIR VKNIILSNKH DV VKPAWLL ECFKTKSFVP WQPRFMIHMC PSTKEHFARE YDCYGDSYFI DTDLNQLKEV FSG IKNSNE QTPEEMASLI ADLEYRYSWD CSPLSMFRRH TVYLDSYAVI NDLSTKNEGT RLAI KALEL RFHGAKVVSC LAEGVSHVII GEDHSRVADF KAFRRTFKRK FKILKESWVT DSIDK CELQ EENQYLI |
-Macromolecule #2: DNA chain I
Macromolecule | Name: DNA chain I / type: dna / ID: 2 / Classification: DNA |
---|---|
Source (natural) | Organism: ![]() |
Sequence | String: CGCGCCCAGC TTTCCCAGCT AATAAACTAA AAACTATGCA TGCTCTACTG CTTCTGATCT AGTCGACC |
-Macromolecule #3: DNA chain J
Macromolecule | Name: DNA chain J / type: dna / ID: 3 / Classification: DNA |
---|---|
Source (natural) | Organism: ![]() |
Sequence | String: CGCGCCCAGC TTTCCCAGCT AATAAACTAA AAACATTCGT TCACGTGAGT TCCAGTACAA GTCTGGTC |
-Macromolecule #4: DNA chain K
Macromolecule | Name: DNA chain K / type: dna / ID: 4 / Classification: DNA |
---|---|
Source (natural) | Organism: ![]() |
Sequence | String: GACTAGATCA GAAGCAGTAG AGCATGCATA GTTTTTAGTT TATTGGGCGC G |
-Macromolecule #5: DNA chain L
Macromolecule | Name: DNA chain L / type: dna / ID: 5 / Classification: DNA |
---|---|
Source (natural) | Organism: ![]() |
Sequence | String: AGACTTGTAC TGGAACTCAC GTGAACGAAT GTTTTTAGTT TATTGGGCGC G |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Concentration | 0.35 mg/mL |
---|---|
Buffer | pH: 7.9 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 42.2 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |