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| 001 | 459716 | ||
| 005 | 20250716150535.0 | ||
| 024 | 7 | _ | |a 10.1107/S2059798321003855 |2 doi |
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| 100 | 1 | _ | |a Norton-Baker, Brenna |0 P:(DE-H253)PIP1090270 |b 0 |
| 245 | _ | _ | |a A simple vapor-diffusion method enables protein crystallization inside the HARE serial crystallography chip |
| 260 | _ | _ | |a Bognor Regis |c 2021 |b Wiley |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a Fixed-target serial crystallography has become an important method for the study of protein structure and dynamics at synchrotrons and X-ray free-electron lasers. However, sample homogeneity, consumption and the physical stress on samples remain major challenges for these high-throughput experiments, which depend on high-quality protein microcrystals. The batch crystallization procedures that are typically applied require time- and sample-intensive screening and optimization. Here, a simple protein crystallization method inside the features of the HARE serial crystallography chips is reported that circumvents batch crystallization and allows the direct transfer of canonical vapor-diffusion conditions to in-chip crystallization. Based on conventional hanging-drop vapor-diffusion experiments, the crystallization solution is distributed into the wells of the HARE chip and equilibrated against a reservoir with mother liquor. Using this simple method, high-quality microcrystals were generated with sufficient density for the structure determination of four different proteins. A new protein variant was crystallized using the protein concentrations encountered during canonical crystallization experiments, enabling structure determination from ∼55 µg of protein. Additionally, structure determination from intracellular crystals grown in insect cells cultured directly in the features of the HARE chips is demonstrated. In cellulo crystallization represents a comparatively unexplored space in crystallization, especially for proteins that are resistant to crystallization using conventional techniques, and eliminates any need for laborious protein purification. This in-chip technique avoids harvesting the sensitive crystals or any further physical handling of the crystal-containing cells. These proof-of-principle experiments indicate the potential of this method to become a simple alternative to batch crystallization approaches and also as a convenient extension to canonical crystallization screens. |
| 536 | _ | _ | |a 632 - Materials – Quantum, Complex and Functional Materials (POF4-632) |0 G:(DE-HGF)POF4-632 |c POF4-632 |f POF IV |x 0 |
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| 700 | 1 | _ | |a Mehrabi, Pedram |0 P:(DE-H253)PIP1029103 |b 1 |
| 700 | 1 | _ | |a Boger, Juliane |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Schoenherr, Robert Frank |0 P:(DE-H253)PIP1030001 |b 3 |
| 700 | 1 | _ | |a von Stetten, David |0 P:(DE-HGF)0 |b 4 |
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| 700 | 1 | _ | |a Kwok, Ashley O. |0 0000-0001-9361-4113 |b 6 |
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| 700 | 1 | _ | |a Schulz, Eike C. |0 P:(DE-HGF)0 |b 10 |e Corresponding author |
| 773 | _ | _ | |a 10.1107/S2059798321003855 |g Vol. 77, no. 6, p. 820 - 834 |0 PERI:(DE-600)2968623-4 |n 6 |p 820 - 834 |t Acta crystallographica / Section D |v 77 |y 2021 |x 2059-7983 |
| 856 | 4 | _ | |u https://scripts.iucr.org/cgi-bin/paper?S2059798321003855 |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/459716/files/A%20simple%20vapor%20diffusion%20method%20enables%20protein%20crystallization%20inside%20the%20HARE%20serial%20crystallography%20chip.pdf |y OpenAccess |
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