Biological Macromolecule Crystallization Database, Version 3.0: new features, data and the NASA archive for protein crystal growth data

Abstract

Version 3.0 of the NIST/NASA/CARB Biological Macromolecule Crystallization Database (BMCD) includes crystal and crystallization data on all forms of biological macromolecules which have produced crystals suitable for X-ray diffraction studies. The data include summary information on each of the macromolecules, crystal data, crystallization conditions and comments about the crystallization procedure if it varies from the traditional methods employed for crystal growth. The database-management software maintains continuity with previous versions providing similar search procedures and displays. Version 3.0 of the BMCD includes protocols and results of crystallization experiments undertaken in space. These new data are comprised of both the NASA Protein Crystal Growth Archive, which includes information on all NASAsponsored protein crystal growth experiments, and data describing other internationally sponsored microgravity macromolecule crystallization studies. The entries for the space growth crystallization experiments contain the crystallization protocols, apparatus descriptions, flight summary data, indication of success or failure of the experiments, references, etc. Other new features of the BMCD include the addition of crystallization procedures for small peptides and cross references to other structural biology databases.

Metal binding to porcine pancreatic elastase: calcium or not calcium

“…In order to resolve this apparent discrepancy, we have crystallized PPE from a sodium sulfate solution as well as from a sulfate-free solution containing sodium citrate and calcium chloride (Gilliland et al, 1994). Based on the bond lengths to their neighbouring O atoms it is dif®cult to differentiate Na + and Ca 2+ (Harding, 1999(Harding, , 2002, but with ten and 18 electrons, the two ions should appear differently in electron-density maps.…”

Crystallization and preliminary crystallographic analysis of the signal recognition particle SRPΦ14‐9 fusion protein

“…A crystallization data base [30] was searched for conditions used for ribosomal proteins, which are also small, basic, RNA binding proteins. The data base aData were collected at the MAD Beamline: BL19 (D-14) at the ESRF using 0.927 A radiation.…”

Trends and Challenges in Experimental Macromolecular Crystallography

“…A Biological Macromolecule Crystallization database facilitates access to macromolecular crystallization procedures and conditions for over 2300 crystal forms (Gilliland et al 1994). …”