Crystals were grown by sitting or hanging drop vapor diffusion at 22 °C. Inactive nmr aCDase crystallized in 100 mM MES pH 6.0, 10% glycerol, 5% PEG 1000 and 30 % PEG 600. Inactive cmw aCDase crystals were obtained in 100 mM citric acid pH 3.5 and 3 M NaCl. Autocleaved human-aCDase was incubated with 1 mM ceranib-2 (Sigma) and 1 mM Triton X-100, and crystallized in 100 mM sodium phosphate-citrate pH 4.3, 200 mM Li2SO4, and 20% PEG 1000. Crystals were soaked in well-solution supplemented with 20% glycerol and heavy atom compounds: 500 mM NaI for nmr protein crystals (20 s) or 500 mM lithium 5-amino-2,4,6-triiodoisophthalate for the cmw homolog (20 s). X-ray diffraction data were collected at 100 K on beamline 08ID-1 with a Rayonix MX300 CCD detector or on beamline 08B1-1 with a Rayonix MX300HE CCD detector at the Canadian Macromolecular Crystallography Facility, Canadian Light Source. Data were processed by HKL200060 (link).
Mx300he ccd detector
Manufactured by Rayonix
Sourced in United States
The MX300HE CCD detector is a high-energy X-ray detector designed for use in various scientific applications. It features a compact and robust design, with a large active area for efficient data collection. The detector utilizes a CCD (Charge-Coupled Device) sensor to capture X-ray images, providing high-resolution data for analysis.
Automatically generated - may contain errors
Lab products found in correlation
3 protocols using mx300he ccd detector
1
Crystallographic Analysis of Acid Ceramidase
2
Cryogenic X-ray Diffraction Crystallography
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
The selected crystals were harvested and immersed in cryoprotectant solution consisting of 30%(v/v) glycerol in mother liquor. The soaked crystal was collected using a Cryo-Loop (Hampton Research, Aliso Viejo, California, USA) and immediately flash-cooled under a stream of nitrogen gas at −173°C. X-ray diffraction data for a single crystal measurement were collected using an MX-300HE CCD detector (Rayonix, Evanston, Illinois, USA) on the SPring-8 BL44XU beamline (Hyogo, Japan). The diffraction data set extended to 1.68 Å resolution and was collected at a wavelength of 0.9 Å. The crystal-to-detector distance was 220 mm. The crystal was rotated 180° with an oscillation angle of 0.5° per frame. The data collected from diffraction measurements were merged, indexed, integrated and scaled using the programs in the HKL-2000 software package (Otwinowski & Minor, 1997 ▶ ). Data-collection statistics are presented in Table 1 ▶ .
3
SARS-CoV PL^pro Structural Analysis
Check if the same lab product or an alternative is used in the 5 most similar protocols
+ Expand
X-ray diffraction data was collected at 100 K on the SPXF beamline 15A1 at the National Synchrotron Radiation Research Center, Taiwan, ROC using a Rayonix MX300HE CCD detector at a wavelength of 1 Å. The diffraction images were processed and then scaled with the HKL-2000 package (Otwinowski and Minor, 1997 ). The structure was solved by the molecular-replacement method with Phaser (McCoy et al., 2007 (link)) using the structure of wild-type SARS-CoV PLpro (PDB entry 2fe8; (Ratia et al., 2006 (link))) as the search model. Manual rebuilding of the structure model was performed with Coot (Emsley and Cowtan, 2004 (link)). Structure refinement was carried out with REFMAC (Murshudov et al., 2011 (link)). Data-processing and refinement statistics are summarized in Table 3 . The crystal structures of the SARS-CoV PLpro-βME complex and SARS-CoV PLpro-glycerol complex have been deposited in the Protein Data Bank (PDB entries 5y3q and 5y3e for PLpro-βME and PLpro-glycerol, respectively).
About PubCompare
Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.
We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.
However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.
Ready to get started?
Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required
Revolutionizing how scientists
search and build protocols!