PDBsum entry 3cqa

Hormone

PDB id: 3cqa

Contents

Protein chains

140 a.a. *

Ligands

SO4 ×2

FMT ×2

Waters ×220

* Residue conservation analysis

PDB id:

3cqa

Name:

Hormone

Title:

Crystal structure of human fibroblast growth factor-1 with mutations glu81ala and lys101ala

Structure:

Heparin-binding growth factor 1. Chain: a, b. Fragment: unp residues 16-152. Synonym: hbgf-1, acidic fibroblast growth factor, afgf, beta- endothelial cell growth factor, ecgf- beta. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Gene: fgf1, fgfa. Expressed in: escherichia coli.

Resolution:

1.80Å R-factor: 0.191 R-free: 0.212

Authors:

A.K.Meher,E.Honjo,R.Kuroki,J.Lee,T.Somasundaram,M.Blaber

Key ref:

A.K.Meher et al. (2009). Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1. Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 1136-1140. PubMed id: 19923735

Date:

02-Apr-08 Release date: 07-Apr-09

Protein chains

P05230  (FGF1_HUMAN) -  Fibroblast growth factor 1 from Homo sapiens

Seq: 155 a.a.

Struc: 140 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

Acta Crystallogr Sect F Struct Biol Cryst Commun 65:1136-1140 (2009)

PubMed id: 19923735

Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1.

A.K.Meher, S.I.Blaber, J.Lee, E.Honjo, R.Kuroki, M.Blaber.

ABSTRACT

Large-volume protein crystals are a prerequisite for neutron diffraction studies and their production represents a bottleneck in obtaining neutron structures. Many protein crystals that permit the collection of high-resolution X-ray diffraction data are inappropriate for neutron diffraction owing to a plate-type morphology that limits the crystal volume. Human fibroblast growth factor 1 crystallizes in a plate morphology that yields atomic resolution X-ray diffraction data but has insufficient volume for neutron diffraction. The thin physical dimension has been identified as corresponding to the b cell edge and the X-ray structure identified a solvent-mediated crystal contact adjacent to position Glu81 that was hypothesized to limit efficient crystal growth in this dimension. In this report, a series of mutations at this crystal contact designed to both reduce side-chain entropy and replace the solvent-mediated interface with direct side-chain contacts are reported. The results suggest that improved crystal growth is achieved upon the introduction of direct crystal contacts, while little improvement is observed with side-chain entropy-reducing mutations alone.