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Acta Crystallographica Section D-Biological Crystallography
ISSN:
Disciplines
(Field of Science):
- biomedical engineering (Engineering and Technology)
- materials engineering (Engineering and Technology)
- medical biology (Medical and Health Sciences )
- pharmacology and pharmacy (Medical and Health Sciences )
- food and nutrition technology (Agricultural sciences)
- biotechnology (Natural sciences)
- biological sciences (Natural sciences)
- chemical sciences (Natural sciences)
(Field of Science)
Ministry points: Help
| Year | Points | List |
|---|---|---|
| Year 2024 | 100 | Ministry scored journals list 2024 |
| Year | Points | List |
|---|---|---|
| 2024 | 100 | Ministry scored journals list 2024 |
| 2023 | 100 | Ministry Scored Journals List |
| 2022 | 100 | Ministry Scored Journals List 2019-2022 |
| 2021 | 100 | Ministry Scored Journals List 2019-2022 |
| 2020 | 100 | Ministry Scored Journals List 2019-2022 |
| 2019 | 100 | Ministry Scored Journals List 2019-2022 |
| 2018 | 45 | A |
| 2017 | 45 | A |
| 2016 | 45 | A |
| 2014 | 45 | A |
| 2013 | 40 | A |
| 2012 | 35 | A |
| 2011 | 35 | A |
| 2010 | 32 | A |
Model:
Points CiteScore:
| Year | Points |
|---|---|
| Year 2023 | 4.5 |
| Year | Points |
|---|---|
| 2023 | 4.5 |
| 2022 | 7.5 |
| 2021 | 10.2 |
| 2020 | 8.9 |
| 2019 | 6.6 |
| 2018 | 6.8 |
| 2017 | 6.4 |
| 2016 | 6 |
| 2015 | 5.5 |
| 2014 | 8.8 |
| 2013 | 19.1 |
| 2012 | 23.1 |
| 2011 | 15.3 |
Impact Factor:
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Papers published in journal
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total: 3
Catalog Journals
Year 2022
Year 2016
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Structural studies of a cold-adapted dimeric Beta-D-galactosidase from Paracoccus sp. 32d
PublicationThe crystal structure of a novel dimeric [beta]-D-galactosidase from Paracoccus sp. 32d (Par[beta]DG) was solved in space group P212121 at a resolution of 2.4 Å by molecular replacement with multiple models using the BALBES software. This enzyme belongs to glycoside hydrolase family 2 (GH2), similar to the tetrameric and hexameric [beta]-D-galactosidases from Escherichia coli and Arthrobacter sp. C2-2, respectively. It is the second...
Year 2012
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Dimeric structure of the N-terminal domain of PriB protein from Thermoanaerobacter tengcongensis solved ab initio
PublicationPriB is one of the components of the bacterial primosome, which catalyzes the reactivation of stalled replication forks at sites of DNA damage. The N-terminal domain of the PriB protein from the thermophilic bacterium Thermoanaerobacter tengcongensis (TtePriB) was expressed and its crystal structure was solved at the atomic resolution of 1.09 Å by direct methods. The protein chain, which encompasses the first 104 residues of the...
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