Subscribe to this collection to receive daily e-mail notification of new additions

Issue Date	Title	Author(s)
Jul-2022	The unintended crystallization of proteins which generally originate from the expression host instead of the target recombinant proteins is periodically reported. Despite the massive technological advances in the field, assigning a structural model to the corresponding diffraction data is not a trivial task. Here, the structure of acyl-carrier protein synthase (AcpS) from Mycobacterium smegmatis (msAcpS), which crystallized inadvertently in an experimental setup to grow crystals of a Mycobacterium tuberculosis protein using M. smegmatis as an expression system, is reported. After numerous unsuccessful attempts to solve the structure of the target protein by the molecular-replacement method no convincing solutions were obtained, indicating that the diffraction data may correspond to a crystal of an artifactual protein, which was finally identified by the Sequence-Independent Molecular replacement Based on Available Databases (SIMBAD) server. The msAcpS structure was solved at 2.27 Å resolution and structural analysis showed an overall conserved fold. msAcpS formed a trimeric structure similar to those of other reported structures of AcpS from various organisms; however, the residues involved in trimer formation are not strictly conserved. An unrelated metal ion (Ni2+), which was possibly incorporated during protein purification, was observed in the proximity of His49 and His116. Structural and sequence differences were observed in the loop connecting the α3 and α4 helices that is responsible for the open and closed conformations of the enzyme. Moreover, the structural analysis of msAcpS augments the current understanding of this enzyme, which plays a crucial role in the functional activation of acyl-carrier proteins in the fatty-acid biosynthesis pathway.	Biswal, Bichitra K; Bhatia, Indu; Yadav, Savita
Jul-2022	Identification, structure determination and analysis of Mycobacterium smegmatis acyl-carrier protein synthase (AcpS) crystallized serendipitously	-
Jan-2016	Crystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities	Biswal, Bichitra Kumar; Nasir, Nazia; Anant, Avishek; Vyas, Rajan
Sep-2018	The crystal structure of an essential high-temperature requirement protein HtrA1 (Rv1223) from Mycobacterium tuberculosis reveals its unique features	Biswal, Bichitra Kumar; Singh, Khundrakpam Herojit; Yadav, Savita; Kumar, Deepak
Jul-2017	Characterization of a secretory hydrolase from Mycobacterium tuberculosis sheds critical insight into host lipid utilization by M. tuberculosis	Biswal, Bichitra Kumar; Singh, Khundrakpam Herojit; Jha, Bhavya; Dwivedy, Abhisek; Choudhary, Eira; G N, Arpitha; Ashraf, Anam; Arora, Divya; Agarwal, Nisheeth
Jun-2018	Identification and structural characterization of a histidinol phosphate phosphatase from Mycobacterium tuberculosis	Biswal, Bichitra Kumar; Jha, Bhavya; Kumar, Deepak; Sharma, Arun; Dwivedy, Abhisek; Singh, Ramandeep
Nov-2020	Crystal structure of the GDP-bound GTPase domain of Rab5a from Leishmania donovani	Biswal, Bichitra K; Pohl, Ehmke; Arora, Ashish; Zohib, Muhammad; Maheshwari, Diva; Pal, Ravi Kant; Freitag-Pohl, Stefanie
Mar-2021	De novo histidine biosynthesis protects Mycobacterium tuberculosis from host IFN-γ mediated histidine starvation	Biswal, Bichitra K; Dwivedy, Abhisek; Ashraf, Anam; Jha, Bhavya; Kumar, Deepak; Agarwal, Nisheeth
Jul-2019	Structural insights into the substrate specificity of SP_0149, the substrate-binding protein of a methionine ABC transporter from Streptococcus pneumoniae	Biswal, Bichitra K; Jha, Bhavya; Vyas, Rajan; Bhushan, Jaya; Sehgal, Devinder
Jul-2020	Prediction of Small Molecule Inhibitors Targeting the Severe Acute Respiratory Syndrome Coronavirus-2 RNA-dependent RNA Polymerase	Biswal, Bichitra K; Jeyakanthan, Jeyaraman; Kar, Deepsikha; Tiwari, Satish; Ahmad, Mohammed; Dwivedy, Abhisek; Mariadasse, Richard
Sep-2018	Serendipitous crystallization and structure determination of bacterioferritin from Achromobacter	Biswal, Bichitra Kumar; Singh, Khundrakpam Herojit; Kumar, Deepak; Jha, Bhavya; Ashraf, Anam; Dwivedy, Abhisek; Ahmad, Mohammed
Nov-2018	Structural and functional characterization of the transcriptional regulator Rv3488 of Mycobacterium tuberculosis H37Rv	Biswal, Bichitra Kumar; Kumari, Meera; Pal, Ravi Kant; Mishra, Alok K.; Tripathi, Sarita; Srivastava, Kishore K; Arora, Ashish
Dec-2013	Structures of native, substrate-bound and inhibited forms of Mycobacterium tuberculosis imidazoleglycerol-phosphate dehydratase	Biswal, Bichitra K; Ahangar, Mohammad Syed; Vyas, Rajan; Nasir, Nazia
Nov-2011	HisB from Mycobacterium tuberculosis: cloning, overexpression in Mycobacterium smegmatis, purification, crystallization and preliminary X-ray crystallographic analysis	Biswal, Bichitra K; Ahangar, Mohammad Syed; Khandokar, Yogesh; Nasir, Nazia; Vyas, Rajan
Apr-2013	Sample preparation, crystallization and structure solution of HisC from Mycobacterium tuberculosis	Biswal, Bichitra K; Nasir, Nazia; Vyas, Rajan
Jan-2012	Molecular cloning, overexpression, purification, crystallization and preliminary X-ray diffraction studies of histidinol phosphate aminotransferase (HisC2) from Mycobacterium tuberculosis	Biswal, Bichitra K; Nasir, Nazia; Vyas, Rajan; Chugh, Chetna; Ahangar, Mohammad Syed
Jul-2014	Overexpression, purification, crystallization and structure determination of AspB, a putative aspartate aminotransferase from Mycobacterium tuberculosis	Biswal, Bichitra K; Saroj, Deepak Chandra; Singh, Khundrakpam Herojit; Anant, Avishek