Comparative studies of ribulose-1,5-biphosphate carboxylase/oxygenase from Alcaligenes eutrophus H16 cells, in the active and CABP-inhibited forms
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference18 articles.
1. Sequence analysis of the Alcaligenes eutrophus chromosomally encoded ribulose bisphosphate carboxylase large and small subunit genes and their gene products
2. The use of sedimentation coefficients to distinguish between models for protein oligomers
3. Calculated sedimentation ratios for assemblies of two, three, four, and five spatially equivalent protomers
4. Influence of the activation state on the sedimentation properties of ribulose bisphosphate carboxylase from Alcaligenes eutrophus.
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. New Insight into the Effects of Various Parameters on the Crystallization of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (RuBisCO) from Alcaligenes eutrophus;Crystals;2022-01-28
2. The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded β-barrel formed by β-strands from four subunits 1 1Edited by R. Huber;Journal of Molecular Biology;1999-05
3. Purification, crystallization and preliminary X-ray studies of two isoforms of Rubisco fromAlcaligenes eutrophus;Acta Crystallographica Section D Biological Crystallography;1999-01-01
4. Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2·4 Å resolution;Journal of Molecular Biology;1990-09
5. Evidence for rapid association-dissociation of ribonuclease T1 from a recombinant strain of Escherichia coli;Journal of Molecular Biology;1989-09
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