Quality Control

From XDSwiki
Revision as of 18:16, 15 March 2008 by Kay (talk | contribs)
Jump to navigation Jump to search

This is an attempt of putting together a number of datasets with different characteristics (high and low resolution, good and bad crystals, untwinned and twinned), their evaluation with different versions of XDS up to the structure solution (as far as that can be done automatically), and the determination of the quality of the resulting data using experimental phasing and refinement.

The goal of this is to find generally optimal parameters for XDS data reduction, to compare new versions of XDS with older ones, and to discover bugs or regressions. At the same time, it serves to display standard procedures for solving crystal structures, which may be used for teaching or learning crystallography.

The metrics I would like to look at is

  • anomalous signal: SHELXC anomalous correlations if two or more wavelengths available; SHELXD (fixed version) success rates and CCall/CCweak maximum values. Clemens Vonrhein additionally suggested anomalous difference fourier peak heights.
  • refinement of a given (known) set of heavy atom positions in (e.g.) SHARP (fixed version): r.m.s. or absolute phase difference, or map correlation w.r.t. phases from good model
  • refinement with (e.g.) refmac5 (fixed version) of a given model, finding LL and R/Rfree

For each project mentioned below, both the raw data and the XDS data reduction is available - links are on the project pages, which are named according to their PDB ids.

The raw data (images) for the different datasets are either available from this site by FTP, or from the (publicly accessible!) JCSG dataset archive.

There's currently data available for

  • PDB id 1T92 (PulG, 2-wl MAD, spacegroup P6522, resolution 2.8 Å)
  • PDB id 1ZTV (JCSG target name TB1631F, 3-wl MAD, resolution 3.1 Å)
  • PDB id 2GIF (AcrB, spacegroup C2, resolution 2.9 Å - a large membrane protein structure)
  • PDB id 1YCE (ATPase C-ring, spacegroup P21, resolution 2.4 Å - a large membrane protein structure, 44-fold NCS, strong diffuse scattering)

I'm working with Qingping Xu on identifying further suitable JCSG datasets. A number of datasets (lysozyme, elastase, ...) will also be made available by Manfred S. Weiss and coworkers.