MX-RDR Macromolecular Xtallography Raw Data Repository
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    468 research outputs found

    Raw X-ray diffraction data for Medicago truncatula omega amidase

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    X-Ray synchrotron diffraction data for Medicago truncatula omega amidase, crystallized in 0.3M sodium nitrate, 0.3M sodium phosphate dibasic, 0.3M Ammonium sulfate, 0.1M sodium HEPES pH 7.5 and 25% MPD, 25% PEG1000, 25% PEG3350. The diffraction images were collected to the resolution of 1.67A at the BESSY II beamline 14.1 in Berlin at 100K using a Pilatus 6M detector. The data was recorded using X-ray wavelength 0.9184A with oscillation angle 0.1° and crystal-to-detector distances 371.14mm

    X-ray diffraction data of NAD-free SAHase from B. elkanii in complex with adenosine

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    Raw X-Ray synchrotron diffraction data for the crystal of NAD-free S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with adenosine. The diffraction images were collected to the resolution of 1.92 Å on the beamline BL14.1 at BESSY, Berlin, at 100 K using a Pilatus 6M detector. The data was recorded in one pass of 3000 images to resolution of 1.92 Å with crystal-to-detector distance 421.32 mm. The direct beam position was: x=1241 px, y=1260 px, oscillation angle was 0.1° and X-ray wavelength equal to 0.9184 Å

    Raw X-ray diffraction data for dimer rabbit muscle phosphoglycerate mutase

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    X-Ray synchrotron diffraction data for rabbit muscle phosphoglycerate mutase, crystallized in PEG4000 with dimes in ASU. The diffraction images were collected to the resolution of 2.5 Å at the BESSY beamline 14.2 in Berlin at 100K using a MX-225 detector. The data was recorded using X-ray wavelength 0.9184 Å with oscillation angle 1° and crystal-to-detector distances 240mm

    Raw X-ray diffraction data for rabbit muscle phosphoglycerate mutase

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    X-Ray synchrotron diffraction data for rabbit muscle phosphoglycerate mutase, crystallized in 0.2M sodium chloride, 0.1M HEPES pH 7.0 and 20% PEG6000. The diffraction images were collected to the resolution of 1.29 Å at the BESSY beamline 14.2 in Berlin at 100K using a MX-225 detector. The data was recorded using X-ray wavelength 0.9184 Å with oscillation angle 0.5° and crystal-to-detector distances 130mm

    X-Ray synchrotron diffraction data for the crystal of Lupinus luteus LlPR-10.2B protein in complex with melatonin and trans-zeatin.

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    X-Ray synchrotron diffraction data (images of .mccd format) for the crystal of Lupinus luteus LlPR-10.2B protein in complex with melatonin and trans-zeatin. The diffraction images were collected to the resolution of 1.57 Å on the beamline I911-2 at the Max LAB synchrotrone (Lund, Sweden) at 100K using a MARMOSAIC 225 mm CCD detector. The data was recorded in one pass of 80 images to resolution of 1.57 Å with crystal-to-detector distance 130 mm. The direct beam position was; x=1562px, y=1494px, oscillation angle was 1° and X-ray wavelength equal to 1.0000 Å

    X-Ray synchrotron diffraction data for the crystal of Lupinus luteus LlPR-10.2B protein in complex with melatonin.

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    X-Ray synchrotron diffraction data (diffraction images of *.img file format) for the crystal of Lupinus luteus LlPR-10.2B protein in complex with melatonin. The diffraction images were collected to the resolution of 1.51 Å on the beamline BL14.1 of synchrotron BESSY (Berlin, Germany) at 100K using a MARMOSAIC 225 mm CCD detector. The data was recorded in one pass of 130 images to resolution of 1.51 Å with crystal-to-detector distance 140 mm. The direct beam position was; x=1536px, y=1532px, oscillation angle was 0.5° and X-ray wavelength equal to 0.918410 Å

    Raw X-ray diffraction data for human muscle fructose-1,6-bisphosphatase in inactive T-state in complex with AMP

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    X-Ray synchrotron diffraction data for human muscle fructose-1,6-bisphosphatase, crystallized in the presence of adenosine monophosphate in the T-state. The diffraction images were collected to the resolution of 1.84 Å at the BESSY beamline 14.2 in Berlin at 100K using a MX-225 detector. The data was recorded using X-ray wavelength 0.827 Å with oscillation angle 0.25° and crystal-to-detector distances 220mm

    Raw X-ray diffraction data of SAHase from Bradyrhizobium elkanii in complex with adenine

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    Raw X-Ray synchrotron diffraction data for the crystal of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii in complex with adenine. The diffraction images were collected to the resolution of 1.95 Å on the beamline BL 14.2 at BESSY, Berlin, at 100 K using a MAR225 detector. The data was recorded in one pass of 200 images to resolution of 1.95 Å with crystal-to-detector distance 190 mm. The direct beam position was: x=1531 px, y=1535 px, oscillation angle was 0.5° and X-ray wavelength equal to 0.918 Å

    Raw X-ray diffraction data for human muscle fructose-1,6-bisphosphatase in inactive T-state

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    X-Ray synchrotron diffraction data for human muscle fructose-1,6-bisphosphatase, crystallized in the presence of adenosine monophosphate in the T-state. Befor measurement crystals were soaked in mother liquor supplemented with 100 mM MgCl2 and 20% (v/v) glycerol to remove AMP. The diffraction images were collected to the resolution of 2.9 Å at the BESSY beamline 14.2 in Berlin at 100K using a MX-225 detector. The data was recorded using X-ray wavelength 0.918 Å with oscillation angle 0.1° and crystal-to-detector distances 280mm

    Raw X-ray diffraction data for human muscle fructose-1,6-bisphosphatase in active R-state

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    X-Ray synchrotron diffraction data for human muscle fructose-1,6-bisphosphatase, crystallized in the R-state without ligand. The diffraction images were collected to the resolution of 1.67 Å at the BESSY beamline 14.1 in Berlin at 100K using a MX-225 detector. The data was recorded using X-ray wavelength 0.918 Å with oscillation angle 0.2° and crystal-to-detector distances 170mm

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