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DOI | 10.1038/s41586-020-2104-4 |
A mechanism of ferritin crystallization revealed by cryo-STEM tomography | |
van Gastel, Nick1,2,3,4,5; Stegen, Steve1,2; Eelen, Guy6,7; Schoors, Sandra6,7; Carlier, Aurelie2,8,9,10; Daniels, Veerle W.11,12; Baryawno, Ninib3,4,5,13; Przybylski, Dariusz14,15; Depypere, Maarten16,17; Stiers, Pieter-Jan1,2; Lambrechts, Dennis2,18,19; Van Looveren, Riet1; Torrekens, Sophie1 | |
2020-02-26 | |
发表期刊 | NATURE |
ISSN | 0028-0836 |
EISSN | 1476-4687 |
出版年 | 2020 |
卷号 | 579期号:7800页码:540-+ |
文章类型 | Article |
语种 | 英语 |
国家 | Israel |
英文关键词 | Protein crystallization is important in structural biology, disease research and pharmaceuticals. It has recently been recognized that nonclassical crystallization involving initial formation of an amorphous precursor phase-occurs often in protein, organic and inorganic crystallization processes(1-5). A two-step nucleation theory has thus been proposed, in which initial low-density, solvated amorphous aggregates subsequently densify, leading to nucleation(4,6,7). This view differs from classical nucleation theory, which implies that crystalline nuclei forming in solution have the same density and structure as does the final crystalline state(1). A protein crystallization mechanism involving this classical pathway has recently been observed directly(8). However, a molecular mechanism of nonclassical protein crystallization(9-15) has not been established(9,11,14). To determine the nature of the amorphous precursors and whether crystallization takes place within them (and if so, how order develops at the molecular level), three-dimensional (3D) molecular-level imaging of a crystallization process is required. Here we report cryogenic scanning transmission microscopy tomography of ferritin aggregates at various stages of crystallization, followed by 3D reconstruction using simultaneous iterative reconstruction techniques to provide a 3D picture of crystallization with molecular resolution. As crystalline order gradually increased in the studied aggregates, they exhibited an increase in both order and density from their surface towards their interior. We observed no highly ordered small structures typical of a classical nucleation process, and occasionally we observed several ordered domains emerging within one amorphous aggregate, a phenomenon not predicted by either classical or two-step nucleation theories. Our molecular-level analysis hints at desolvation as the driver of the continuous order-evolution mechanism, a view that goes beyond current nucleation models, yet is consistent with a broad spectrum of protein crystallization mechanisms. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000527257200001 |
WOS关键词 | NONCLASSICAL NUCLEATION ; PROTEIN ; PRECURSORS ; CLUSTERS ; CRYSTALS ; ORDER |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/281513 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Katholieke Univ Leuven, Lab Clin & Expt Endocrinol, Dept Chron Dis Metab & Ageing, Leuven, Belgium; 2.Katholieke Univ Leuven, Div Skeletal Tissue Engn, Prometheus, Leuven, Belgium; 3.Harvard Univ, Dept Stem Cell & Regenerat Biol, Cambridge, MA 02138 USA; 4.Harvard Univ, Harvard Stem Cell Inst, Cambridge, MA 02138 USA; 5.Massachusetts Gen Hosp, Ctr Regenerat Med, Boston, MA 02114 USA; 6.Katholieke Univ Leuven, Lab Angiogenesis & Vasc Metab, Dept Oncol, Leuven, Belgium; 7.VIB, Lab Angiogenesis & Vasc Metab, Ctr Canc Biol, Leuven, Belgium; 8.Katholieke Univ Leuven, Biomech Sect, Dept Mech Engn, Leuven, Belgium; 9.Univ Liege, Biomech Res Unit, GIGA Silico Med, Liege, Belgium; 10.Maastricht Univ, MERLN Inst Technol Inspired Regenerat Med, Maastricht, Netherlands; 11.Katholieke Univ Leuven, Lab Lipid Metab & Canc, Dept Oncol, Leuven, Belgium; 12.Harvard Med Sch, Dana Farber Canc Inst, Dept Med Oncol, Boston, MA 02115 USA; 13.Karolinska Inst, Dept Childrens & Womens Hlth, Childhood Canc Res Unit, Stockholm, Sweden; 14.Brandeis Univ, Howard Hughes Med Inst, Waltham, MA 02254 USA; 15.Brandeis Univ, Dept Biol, Waltham, MA 02254 USA; 16.Katholieke Univ Leuven, Med Imaging Res Ctr, Leuven, Belgium; 17.Katholieke Univ Leuven, Dept Elect Engn, Med Image Comp, ESAT PSI, Leuven, Belgium; 18.Katholieke Univ Leuven, Dept Microbial & Mol Syst, Ctr Surface Chem & Catalysis, Leuven, Belgium; 19.Katholieke Univ Leuven, Dept Dev & Regenerat, Tissue Engn Lab, Skeletal Biol & Engn Res Ctr, Leuven, Belgium; 20.Katholieke Univ Leuven, Lab Cell Death Res & Therapy, Dept Cellular & Mol Med, Leuven, Belgium; 21.Katholieke Univ Leuven, Lab Translat Genet, Dept Human Genet, Leuven, Belgium; 22.Katholieke Univ Leuven, Lab Funct Epigenet, Dept Human Genet, Leuven, Belgium; 23.VIB, Lab Translat Genet, Ctr Canc Biol, Leuven, Belgium |
推荐引用方式 GB/T 7714 | van Gastel, Nick,Stegen, Steve,Eelen, Guy,et al. A mechanism of ferritin crystallization revealed by cryo-STEM tomography[J]. NATURE,2020,579(7800):540-+. |
APA | van Gastel, Nick.,Stegen, Steve.,Eelen, Guy.,Schoors, Sandra.,Carlier, Aurelie.,...&Torrekens, Sophie.(2020).A mechanism of ferritin crystallization revealed by cryo-STEM tomography.NATURE,579(7800),540-+. |
MLA | van Gastel, Nick,et al."A mechanism of ferritin crystallization revealed by cryo-STEM tomography".NATURE 579.7800(2020):540-+. |
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