![]() | EMDB-1409![]() ![]() ![]() ![]() The EM structure of human DNA polymerase gamma reveals a localized contact between the catalytic and accessory subunits. |
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![]() | EMDB-1410![]() ![]() ![]() ![]() The EM structure of human DNA polymerase gamma reveals a localized contact between the catalytic and accessory subunits. |
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![]() | EMDB-1399![]() ![]() ![]() ![]() Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. |
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![]() | EMDB-1400![]() ![]() ![]() ![]() Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. |
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![]() | EMDB-1401![]() ![]() ![]() ![]() Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. |
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![]() | EMDB-1402![]() ![]() ![]() ![]() Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. |
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![]() | EMDB-1403![]() ![]() ![]() ![]() Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. |
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![]() | EMDB-1404![]() ![]() ![]() ![]() Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. |
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![]() | EMDB-1405![]() ![]() ![]() ![]() Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. |
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![]() | EMDB-1406![]() ![]() ![]() ![]() Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. |
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![]() | EMDB-1407![]() ![]() ![]() ![]() Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. |
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![]() | EMDB-1408![]() ![]() ![]() ![]() Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. |
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![]() | EMDB-1397![]() ![]() ![]() ![]() Multiple states of a nucleotide-bound group 2 chaperonin. |
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![]() | EMDB-1398![]() ![]() ![]() ![]() Multiple states of a nucleotide-bound group 2 chaperonin. |
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![]() | EMDB-1395![]() ![]() ![]() ![]() Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy. |
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![]() | EMDB-1394![]() ![]() ![]() ![]() Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. |
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![]() | EMDB-1393![]() ![]() ![]() ![]() Cryo-EM study of the Pseudomonas bacteriophage phiKZ. |
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![]() | EMDB-1414![]() ![]() ![]() ![]() Molecular architecture of the prolate head of bacteriophage T4. |
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![]() | EMDB-1396![]() ![]() ![]() ![]() Multiple states of a nucleotide-bound group 2 chaperonin. |
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![]() | EMDB-1392![]() ![]() ![]() ![]() A three-dimensional cryo-electron microscopy structure of the bacteriophage phiKZ head. |
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![]() | EMDB-1376![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1377![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1378![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1379![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1380![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1381![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1382![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1383![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1384![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1385![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1386![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1387![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1388![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1389![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1390![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1375![]() ![]() ![]() ![]() Averaging tens to hundreds of icosahedral particle images to resolve protein secondary structure elements using a Multi-Path Simulated Annealing optimization algorithm. |
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![]() | EMDB-1391![]() ![]() ![]() ![]() Structured mRNAs regulate translation initiation by binding to the platform of the ribosome. |
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![]() | EMDB-1374![]() ![]() ![]() ![]() The molecular architecture of cadherins in native epidermal desmosomes. |
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![]() | EMDB-1372![]() ![]() ![]() ![]() Architecture of the Dam1 kinetochore ring complex and implications for microtubule-driven assembly and force-coupling mechanisms. |
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![]() | EMDB-1373![]() ![]() ![]() ![]() Architecture of the Dam1 kinetochore ring complex and implications for microtubule-driven assembly and force-coupling mechanisms. |
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![]() | EMDB-1371![]() ![]() ![]() ![]() Architecture of the Dam1 kinetochore ring complex and implications for microtubule-driven assembly and force-coupling mechanisms. |
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![]() | EMDB-1424![]() ![]() ![]() ![]() The structure of the prokaryotic cyclic nucleotide-modulated potassium channel MloK1 at 16 A resolution. |
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![]() | EMDB-1369![]() ![]() ![]() ![]() Progression of the ribosome recycling factor through the ribosome dissociates the two ribosomal subunits. |
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![]() | EMDB-1370![]() ![]() ![]() ![]() Progression of the ribosome recycling factor through the ribosome dissociates the two ribosomal subunits. |
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![]() | EMDB-1367![]() ![]() ![]() ![]() Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution. |
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![]() | EMDB-1366![]() ![]() ![]() ![]() Locking and unlocking of ribosomal motions. |
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![]() | EMDB-1363![]() ![]() ![]() ![]() Locking and unlocking of ribosomal motions. |
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![]() | EMDB-1364![]() ![]() ![]() ![]() Locking and unlocking of ribosomal motions. |
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![]() | EMDB-1365![]() ![]() ![]() ![]() Locking and unlocking of ribosomal motions. |
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![]() | EMDB-1362![]() ![]() ![]() ![]() Locking and unlocking of ribosomal motions. |
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