Works matching IS 2053230X AND DT 2019 AND VI 75 AND IP 2
Results: 10
Structure of an Influenza A virus N9 neuraminidase with a tetrabrachion‐domain stalk.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 2, p. 89, doi. 10.1107/S2053230X18017892
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- Article
Crystal structure of the aromatic‐amino‐acid aminotransferase from Streptococcus mutans.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 2, p. 141, doi. 10.1107/S2053230X18018472
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High‐resolution structure of a Y27W mutant of the Dishevelled2 DIX domain.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 2, p. 116, doi. 10.1107/S2053230X18018290
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Crystal structure of the programmed cell death 5 protein from Sulfolobus solfataricus.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 2, p. 73, doi. 10.1107/S2053230X18017673
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Structures of the antibody 64M‐5 Fab and its complex with dT(6–4)T indicate induced‐fit and high‐affinity mechanisms.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 2, p. 80, doi. 10.1107/S2053230X18017661
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Crystallization and X‐ray analysis of monodisperse human properdin.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 2, p. 0, doi. 10.1107/S2053230X18018150
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Titration of ionizable groups in proteins using multiple neutron data sets from a single crystal: application to the small GTPase Ras.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 2, p. 111, doi. 10.1107/S2053230X18018125
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Penetration of dyes into protein crystals.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 2, p. 132, doi. 10.1107/S2053230X18018241
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A revisited version of the apo structure of the ligand‐binding domain of the human nuclear receptor retinoic X receptor α.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 2, p. 98, doi. 10.1107/S2053230X18018022
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Iterative screen optimization maximizes the efficiency of macromolecular crystallization.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 2, p. 123, doi. 10.1107/S2053230X18017338
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