Computational protocol: Mechanistic and functional insights into fatty acid activation in Mycobacterium tuberculosis

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Protocol publication

[…] Crystallization of the N-terminal domain, comprising of the first 460 residues of FAAL28, was performed by hanging drop vapor diffusion method. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.97, b = 60.74, c = 136.54 angstroms. The crystal structure of the N-terminal domain of FAAL28 at 2.35 angstroms resolution has been solved using the MAD method (see online). Model building was performed using O version 10.0.0.. After several rounds of iterative manual model building and refinement using CNS version 1.2, the structure has been refined to a final Rcryst and Rfree of 20.7% and 26.7% respectively. The following short segments (1-3, 97-102, 131-137, 153-160 and 172-177 of subdomain A, 203-204 connecting subdomains A and B, 367-368 which are part of the FAAL specific insertion and 460 last residue at C-terminus) are missing in the electron density presumably due to disorder and hence are not modeled. The quality of the model was checked using PROCHECK. The ribbon figures were made by SETOR and multiple sequence alignment was prepared using ALSCRIPT […]

Pipeline specifications

Software tools CNS, PROCHECK
Application Protein structure analysis
Organisms Mycobacterium tuberculosis
Diseases Tuberculosis
Chemicals Acyl Coenzyme A, Cyclic AMP