Literature DB >> 26917153

Protein crystallography beamline (PX-BL21) at Indus-2 synchrotron.

Ashwani Kumar1, Biplab Ghosh1, H K Poswal1, K K Pandey1, M V Hosur2, Abhilash Dwivedi1, Ravindra D Makde1, Surinder M Sharma1.   

Abstract

The protein crystallography beamline (PX-BL21), installed at the 1.5 T bending-magnet port at the Indian synchrotron (Indus-2), is now available to users. The beamline can be used for X-ray diffraction measurements on a single crystal of macromolecules such as proteins, nucleic acids and their complexes. PX-BL21 has a working energy range of 5-20 keV for accessing the absorption edges of heavy elements commonly used for phasing. A double-crystal monochromator [Si(111) and Si(220)] and a pair of rhodium-coated X-ray mirrors are used for beam monochromatization and manipulation, respectively. This beamline is equipped with a single-axis goniometer, Rayonix MX225 CCD detector, fluorescence detector, cryogenic sample cooler and automated sample changer. Additional user facilities include a workstation for on-site data processing and a biochemistry laboratory for sample preparation. In this article the beamline, other facilities and some recent scientific results are briefly described.

Entities:  

Keywords:  Indus-2; beamline; bending magnet; protein crystallography

Mesh:

Substances:

Year:  2016        PMID: 26917153     DOI: 10.1107/S160057751600076X

Source DB:  PubMed          Journal:  J Synchrotron Radiat        ISSN: 0909-0495            Impact factor:   2.616


  8 in total

1.  Carboxypeptidase in prolyl oligopeptidase family: Unique enzyme activation and substrate-screening mechanisms.

Authors:  Pooja Yadav; Venuka Durani Goyal; Neeraj Kailash Gaur; Ashwani Kumar; Sadashiv M Gokhale; Sahayog N Jamdar; Ravindra D Makde
Journal:  J Biol Chem       Date:  2018-11-08       Impact factor: 5.157

2.  Crystal structure of XCC3289 from Xanthomonas campestris: homology with the N-terminal substrate-binding domain of Lon peptidase.

Authors:  Rahul Singh; Sonali Deshmukh; Ashwani Kumar; Venuka Durani Goyal; Ravindra D Makde
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2020-09-16       Impact factor: 1.056

3.  Structure of Yak Lactoperoxidase at 1.55 Å Resolution.

Authors:  V Viswanathan; Chitra Rani; Nayeem Ahmad; Prashant Kumar Singh; Pradeep Sharma; Punit Kaur; Sujata Sharma; Tej P Singh
Journal:  Protein J       Date:  2021-01-03       Impact factor: 2.371

4.  Structure of the human aminopeptidase XPNPEP3 and comparison of its in vitro activity with Icp55 orthologs: Insights into diverse cellular processes.

Authors:  Rahul Singh; Sahayog N Jamdar; Venuka Durani Goyal; Ashwani Kumar; Biplab Ghosh; Ravindra D Makde
Journal:  J Biol Chem       Date:  2017-05-05       Impact factor: 5.157

5.  Structure and dynamics of Type III periplasmic proteins VcFhuD and VcHutB reveal molecular basis of their distinctive ligand binding properties.

Authors:  Shubhangi Agarwal; Sanjay Dey; Biplab Ghosh; Maitree Biswas; Jhimli Dasgupta
Journal:  Sci Rep       Date:  2017-02-20       Impact factor: 4.379

6.  Structural basis of inactivation of human counterpart of mouse motor neuron degeneration 2 mutant in serine protease HtrA2.

Authors:  Ajay R Wagh; Kakoli Bose
Journal:  Biosci Rep       Date:  2018-10-05       Impact factor: 3.840

7.  Phylogenetic and crystallographic analysis of Nostoc phycocyanin having blue-shifted spectral properties.

Authors:  Ravi R Sonani; Rajesh Prasad Rastogi; Stuti Nareshkumar Patel; Mukesh Ghanshyam Chaubey; Niraj Kumar Singh; Gagan D Gupta; Vinay Kumar; Datta Madamwar
Journal:  Sci Rep       Date:  2019-07-08       Impact factor: 4.379

8.  Structure of a 14-3-3ε:FOXO3apS253 Phosphopeptide Complex Reveals 14-3-3 Isoform-Specific Binding of Forkhead Box Class O Transcription Factor (FOXO) Phosphoproteins.

Authors:  Subashini Mathivanan; Puneeth Kumar Chunchagatta Lakshman; Manvi Singh; Saranya Giridharan; Keerthana Sathish; Manjunath A Hurakadli; Kavitha Bharatham; Neelagandan Kamariah
Journal:  ACS Omega       Date:  2022-07-05
  8 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.