Crystallization and structural studies of components of the protein-synthesizing system from Thermus thermophilus

Garber, M.B.; Davydova, Natalia; Eliseikina, I.A.; Fomenkova, N.P.; Gryaznova, O.I.; Gryshkovskaya, I.; Nevskaya, N.; Nikonov, S.V.; Rak, Alexey; Sedelnikova, Svetlana E.; Serganov, Alexander; Shcherbakov, Dmitry; Tishchenko, Svetlana; Vysotskaya, Valentina S; Zheltonosova, J.; Liljas, Anders; Aevarsson, Arnthór; Al-Karadaghi, Salam

doi:10.1016/0022-0248(96)00337-5

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Crystallization and Preparation Of Heavy-atom Derivatives1

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Cited by 3 publications

(2 citation statements)

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“…EF-G from T. thermophilus was purified and crystallized using the hanging drop technique as described earlier [35], with some minor modifications to the crystallization procedure [36]. Magnesium sulphate was present at a concentration of 3 mM.…”

Section: Methodsmentioning

confidence: 99%

The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange

Al-Karadaghi¹,

Aevarsson²,

Garber

et al. 1996

Structure

127

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Section: Methodsmentioning

confidence: 99%

The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange

Al-Karadaghi¹,

Aevarsson²,

Garber

et al. 1996

Structure

127

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“…The crystals were fragile and unstable in different storage solutions. To overcome this problem they were cross-linked with 0.25% glutaraldehyde [22]. Isomorphous heavy-atom derivatives were obtained by soaking crystals in the standard solution: 10% PEG 10000, 50 mM Hepes, pH 7.5, to which heavy-atom compounds were added (Table 1).…”

Section: Crystallization and Preparation Of Heavy-atom Derivativesmentioning

confidence: 99%

Archaeal ribosomal protein L1: the structure provides new insights into RNA binding of the L1 protein family

et al. 2000

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The unusually high RNA-binding affinity of MjaL1 might be explained by the exposure of its highly conserved regions. The open conformation of MjaL1 is strongly stabilized by nonconserved interdomain interactions and suggests that the closed conformations of L1 (as in TthL1) open upon RNA binding. Comparison of the two L1 protein structures reveals a high conformational variability of this ribosomal protein. Determination of the MjaL1 structure offers an additional variant for fitting the L1 protein into electron-density maps of the 50S ribosomal subunit.

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Structural Studies of Ribosomal Proteins

Nikonov¹,

Nevskaya²,

Fedorov³

et al. 1998

BCHM

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Crystal and solution structures of fourteen ribosomal proteins from thermophilic bacteria have been determined during the last decade. This paper reviews structural studies of ribosomal proteins from Thermus thermophilus carried out at the Institute of Protein Research (Pushchino, Russia) in collaboration with the University of Lund (Lund, Sweden) and the Center of Structural Biochemistry (Karolinska Institute, Huddinge, Sweden). New experimental data on the crystal structure of the ribosomal protein L30 from T. thermophilus are also included.

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Crystallization and structural studies of components of the protein-synthesizing system from Thermus thermophilus

Cited by 3 publications

References 39 publications

The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange

The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange

Archaeal ribosomal protein L1: the structure provides new insights into RNA binding of the L1 protein family

Structural Studies of Ribosomal Proteins

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