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raxis iv ip  (Rigaku Corporation)


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    Structured Review

    Rigaku Corporation raxis iv ip
    Raxis Iv Ip, supplied by Rigaku Corporation, used in various techniques. Bioz Stars score: 97/100, based on 1428 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/raxis+iv+++ip/MicroMax-007+HF/10__1042_slash_bcj20180605-52-20-14
    Average 97 stars, based on 1428 article reviews
    raxis iv ip - by Bioz Stars, 2026-10
    97/100 stars

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    other:

    Article Title: New structural insights into anomeric carbohydrate recognition by frutalin: an α-<scp>d</scp>-galactose-binding lectin from breadfruit seeds
    Article Snippet: Antonio Eufrásio Vieira Neto, Felipe Domingos de Sousa, Humberto D’Muniz Pereira, Frederico Bruno Mendes Batista Moreno, Marcos Roberto Lourenzoni, Thalles Barbosa Grangeiro, Ana Cristina de Oliveira Monteiro Moreira and Renato de Azevedo Moreira Department of Biochemistry and Molecular Biology, Federal University of Ceará, Campus do Pici, Bloco 907, Fortaleza, Ceara 60451 970, Brazil; Center of Experimental Biology (Nubex), University of Fortaleza (UNIFOR), Av.. Washington Soares, 1321, Fortaleza, Ceara 60811-905, Brazil; Physics Institute of São Carlos, University of São Paulo, Av.. Trabalhador São-Carlense, 400 — Pq.



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    Statistics of data collection and structure refinement

    Journal:

    Article Title: Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 ? resolution

    doi:

    Figure Lengend Snippet: Statistics of data collection and structure refinement

    Article Snippet: The statistics of the data collection were judged to be fit for use as listed in Table 1 . table ft1 table-wrap mode="anchored" t5 Table 1. caption a7 Enzyme Wild type F120A F120G F120W Data collection Space group P3 2 21 Unit cell dimension (Å) a = b = 64.05, c = 63.36 a = b = 63.66, c = 63.49 a = b = 63.73, c = 63.49 a = b = 63.90, c = 63.33 (deg) γ = 120 γ = 120 γ = 120 γ = 120 X-ray source SPring-8 BL40B2 SPring-8 BL44B2 SPring-8 BL40B2 SPring-8 BL44B2 Wavelength (Å) 0.968641 0.7 0.7 0.7 Detector Rigaku RAXIS IV++ IP ADSC Quantum 4R CCD Rigaku RAXIS IV ++ IP ADSC Quantium 4D CCD Mount Cryo protectant (300 mg/ml trehalose) Maximum resolution (Å) 1.35 1.00 1.20 1.00 Data collection resolution (Å) 55.5–1.35 16.8–1.00 41.7–1.20 16.8–1.00 Number of total reflections 241,908 1,446,353 404,905 886,320 Number of unique reflections 33,471 80,089 41,727 80,099 Completeness (%) 98.8 99.7 88.8 99.6 Average I/σ 14.3 36.9 12.6 34.9 R merge 0.05 0.07 0.04 0.06 Structure refinement Refinement resolution (Å) 6.00–1.40 5.00–1.40 6.00–1.40 6.00–1.40 R-factor 0.204 0.201 0.210 0.218 R-free 0.242 0.254 0.265 0.272 RMS (bond distances) (Å) 1.2 1.2 1.1 1.2 RMS (bond angle) (deg) 0.006 0.005 0.005 0.005 Open in a separate window Statistics of data collection and structure refinement The structures were refined by rigid-body, positional, slow-cool, and b-refinement in X-PLOR.

    Techniques:

    Statistics of data collection and structure refinement

    Journal:

    Article Title: Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 ? resolution

    doi:

    Figure Lengend Snippet: Statistics of data collection and structure refinement

    Article Snippet: Detector , Rigaku RAXIS IV++ IP , ADSC Quantum 4R CCD , Rigaku RAXIS IV ++ IP , ADSC Quantium 4D CCD.

    Techniques: