The result of all the work described in the previous chapters will be a set of coordinates and other data suitable for deposit in the Protein Data Bank. You or I may use these coordinates, and we need to have some insight into their accuracy and reliability. In the previous chapters, indicators have been described, which may suggest aspects of the data or interpretation procedures that might lead to problems. But as the determination of protein crystal structures becomes more routine, many of these indicators are omitted from publications. Fortunately, crystallographic procedures are self-checking to a large extent. It is rare for a major error of interpretation to lead right through to a published refined structure. A high Rfree factor is a warning, especially if coupled with departures from the requirements of correct bond lengths, angles, and acceptable dihedral angles. On the other hand, there will always be a desire to squeeze more results from the data. All interpretations are subject to error; nearly all protein crystals have regions that are less ordered, where accurate interpretation is less feasible; and the structure may be overrefined, using too many variables for the data. If the majority of the molecule is correctly interpreted, a reasonable R factor may be obtained even though some small regions are completely wrong. During refinement it is usual to restrain the bond lengths and bond angles to be near their theoretical values, as described in Chapter 12. The extent to which bond lengths and bond angles depart from these values is often quoted as an indicator of accuracy. These departures are, however, difficult to interpret because they depend on how tightly the restraints have been applied. The same applies to the restraint of certain coordinates to lie in a plane. This difficulty illustrates a general problem. Designers of refinement procedures are understandably anxious to improve their procedures to lead directly to a well-refined structure. Every aspect of structure that can be recognized as having a regularity could, in principle, be expressed as a restraint which enforces it during refinement.