Computational protocol: Crystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding

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Protocol publication

[…] The 3.1 Å resolution data set contained 100 images with a detector-to-crystal distance of 300 mm, exposure time of 1 s, and oscillation range of 1° per image. The data set was indexed, integrated, and scaled using HKL-2000 software []. The data collection statistics are summarized in . For structure determination of CYP153D17, MR was performed using the program MOLREP in the CCP4 suite [,]. The coordinate of P450pyr hydroxylase from S. macrogoltabida (PDB code, 3RWL) was used for MR searching. The structure model of CYP153D17 was iteratively rebuilt and refined by manually fitting the residues and backbone into the electron density map by using the WinCoot and REFMACK programs from the CCP4 suite [,]. The quality of the refined structure was validated using the MOLPROBITY server and SFCHECK with an Rwork of 26.25% and Rfree of 34.07% [,]. The statistical data for structure refinement are provided in . […]

Pipeline specifications

Software tools HKL-2000, Molrep, CCP4, MolProbity
Application Protein structure analysis
Chemicals Alkanes, Fatty Acids, Hydrocarbons, Myristic Acid