Advances in molecular-replacement procedures: the REVAN pipeline.
The REVAN pipeline aiming at the solution of protein structures via molecular replacement (MR) has been assembled. It is the successor to REVA, a pipeline that is particularly efficient when the sequence identity (SI) between the target and the model is greater than 0.30. The REVAN and REVA procedures coincide when the SI is >0.30, but differ substantially in worse conditions. To treat these cases, REVAN combines a variety of programs and algorithms (REMO09, REFMAC, DM, DSR, VLD, free lunch, Coot, Buccaneer and phenix.autobuild). The MR model, suitably rotated and positioned, is first refined by a standard REFMAC refinement procedure, and the corresponding electron density is then submitted to cycles of DM-VLD-REFMAC. The next REFMAC applications exploit the better electron densities obtained at the end of the VLD-EDM sections (a procedure called vector refinement). In order to make the model more similar to the target, the model is submitted to mutations, in which Coot plays a basic role, and it is then cyclically resubmitted to REFMAC-EDM-VLD cycles. The phases thus obtained are submitted to free lunch and allow most of the test structures studied by DiMaio et al. [(2011), Nature (London), 473, 540-543] to be solved without using energy-guided programs.
Istituto di Cristallografia, CNR, Via G. Amendola 122/o, 70126 Bari, Italy.
Benedetta
B
Carrozzini
Istituto di Cristallografia, CNR, Via G. Amendola 122/o, 70126 Bari, Italy.
Giovanni Luca
GL
Cascarano
Istituto di Cristallografia, CNR, Via G. Amendola 122/o, 70126 Bari, Italy.
Carmelo
C
Giacovazzo
Istituto di Cristallografia, CNR, Via G. Amendola 122/o, 70126 Bari, Italy.
Annamaria
A
Mazzone
D000465:Algorithms; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
D011506:Proteins
REVAN; automated model building; molecular replacement; sequence mutation